Structural biology articles within Nature

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  • Letter |

    This study provides insights into conformational changes that lead to phospho-ubiquitin-induced PARKIN activation and how PARKIN is recruited to phospho-ubiquitin chains on mitochondria; the crystal structure of PARKIN in complex with phospho-ubiquitin also indicates that the pocket within PARKIN where phospho-ubiquitin binds carries amino acid residues that are mutated in patients with autosomal-recessive juvenile Parkinsonism.

    • Tobias Wauer
    • , Michal Simicek
    •  & David Komander

  • Analysis |

    There are ∼800 human GPCRs and 16 different Gα proteins; this study revealed the molecular details of Gα activation by GPCRs and suggests that a universal activation mechanism governs Gα activation—the details of this mechanism can explain how the GPCR–Gα system diversified rapidly, while conserving the allosteric activation mechanism.

    • Tilman Flock
    • , Charles N. J. Ravarani
    •  & M. Madan Babu

  • Article |

    This study determines the structure of the spliceosomal tri-snRNP complex (containing three small nuclear RNAs and more than 30 proteins) by single-particle cryo-electron microscopy; the resolution is sufficient to discern the organization of RNA and protein components involved in spliceosome activation, exon alignment and catalysis.

    • Thi Hoang Duong Nguyen
    • , Wojciech P. Galej
    •  & Kiyoshi Nagai

  • News & Views |

    An enzyme has been found that alters the molecular structure of vitamin B2, adding a fourth ring to its existing three-ring system. The product catalyses new types of chemistry in concert with certain other enzymes. See Letters p.497 & p.502

    • Catherine F. Clarke
    •  & Christopher M. Allan

  • Letter |

    Ubiquinone is an essential component of electron transfer chains found both in bacteria and in mitochondria; the bacterial enzyme UbiX involved in ubiquinone biosynthesis is a flavin prenyltransferase, and the flavin-derived cofactor synthesized by UbiX is used by the UbiD decarboxylase in the ubiquinone biosynthetic pathway.

    • Mark D. White
    • , Karl A. P. Payne
    •  & David Leys

  • Letter |

    Retroviruses such as HIV rely on the intasome, a tetramer of integrase protein bound to the viral DNA ends interacting with host chromatin, for integration into the host genome; the structure of the intasome as it interacts with a nucleosome is now solved, giving insight into the integration process.

    • Daniel P. Maskell
    • , Ludovic Renault
    •  & Peter Cherepanov

  • Review Article |

    Although classical crystallography is insufficient to determine disordered structure in crystals, correlated disorder does nevertheless contain clear crystallographic signatures that map to the type of disorder, which we are learning to decipher.

    • David A. Keen
    •  & Andrew L. Goodwin

  • Article |

    Here the X-ray crystal structures of the Drosophila dopamine transporter bound to dopamine, D-amphetamine, methamphetamine and cocaine are solved; these structures show how a neurotransmitter, small molecule stimulants and cocaine bind to a biogenic amine transporter, and are examples of how the ligand binding site of a neurotransmitter transporter can remodel itself to accommodate structurally unrelated small molecules that are different in shape, size and polarity or charge.

    • Kevin H. Wang
    • , Aravind Penmatsa
    •  & Eric Gouaux

  • Article |

    The structure of the human ribosome at high resolution has been solved; by combining single-particle cryo-EM and atomic model building, local resolution of 2.9 Å was achieved within the most stable areas of the structure.

    • Heena Khatter
    • , Alexander G. Myasnikov
    •  & Bruno P. Klaholz

  • News & Views |

    The TRPA1 ion channel activates pain pathways in response to noxious compounds. The structure of TRPA1 has now been solved, providing insight into how it functions. See Article p.511

    • David E. Clapham

  • Article |

    The crystal structures of the human adiponectin receptors AdipoR1 and AdipoR2 are solved at 2.9 and 2.4 Å resolution, respectively; the structural and functional information may aid the development and optimization of adiponectin receptor agonists for the treatment of obesity-related diseases.

    • Hiroaki Tanabe
    • , Yoshifumi Fujii
    •  & Shigeyuki Yokoyama

  • Article |

    Two X-ray crystal structures are presented of the human P2Y1 G-protein-coupled receptor, which is an important target for anti-thrombotic drugs; the structures unexpectedly reveal two ligand-binding sites.

    • Dandan Zhang
    • , Zhan-Guo Gao
    •  & Beili Wu

  • Outlook |

    Researchers are borrowing tricks from armadillo shells and mother-of-pearl to create replacements for human bone and to develop a new generation of protective clothing.

    • Katharine Sanderson

  • Article |

    dG•dT and rG•rU ‘wobble’ mispairs in DNA and RNA transiently form base pairs with Watson–Crick geometry via tautomerization and ionization with probabilities that correlate with misincorporation probabilities during replication and translation.

    • Isaac J. Kimsey
    • , Katja Petzold
    •  & Hashim M. Al-Hashimi

  • Article |

    The crystal structure of the heterohexameric origin recognition complex (ORC), essential for coordinating DNA replication onset in eukaryotes, is resolved at 3.5 Å resolution.

    • Franziska Bleichert
    • , Michael R. Botchan
    •  & James M. Berger

  • News |

    Reconstruction of mimivirus innards brings X-ray laser images of live cells one step closer.

    • Davide Castelvecchi

  • Letter |

    A single particle cryo-EM structure of the 70S ribosome in complex with the elongation factor Tu breaks the 3 Å resolution barrier of the technique and locally exceeds the resolution of previous crystallographic studies, revealing all modifications in rRNA and explaining their roles in ribosome function and antibiotic binding.

    • Niels Fischer
    • , Piotr Neumann
    •  & Holger Stark

  • Article |

    The crystal structure of the RAG1–RAG2 heterotetramer forms a Y-shaped structure, with each arm containing a RAG1–RAG2 heterodimer; the overall structure is reminiscent of hairpin-forming transposases, attesting to its evolutionary history as a specialized form of a transposition activity.

    • Min-Sung Kim
    • , Mikalai Lapkouski
    •  & Martin Gellert

  • Letter |

    Glycopeptide antibiotics are biosynthesized by non-ribosomal peptide synthetases, which contain a previously uncharacterized ‘X-domain’ now shown to recruit three cytochrome P450 oxygenases that are necessary for the antibiotics to achieve their final, active conformation.

    • Kristina Haslinger
    • , Madeleine Peschke
    •  & Max J. Cryle

  • News & Views |

    Signal sequences on messenger RNA that initiate protein synthesis are not thought to be interchangeable between life's domains. The finding that a signal from an arthropod virus can function in bacteria questions this idea. See Letter p.110

    • Eric Jan

  • Letter |

    A eukaryotic viral internal ribosome entry site (IRES) element is described that binds both bacterial and eukaryotic ribosomes and initiates translation in both, demonstrating that RNA structure-based initiation can occur in both these domains of life, although in bacteria the element uses a mechanism that differs from that in eukaryotes.

    • Timothy M. Colussi
    • , David A. Costantino
    •  & Jeffrey S. Kieft

  • Article |

    An analysis of a bacterial homologue of the human glutamate transporter using single-molecule FRET and X-ray crystallography reveals that opening of the interface between its distinct transport and scaffold domains is rate determining for the transport cycle.

    • Nurunisa Akyuz
    • , Elka R. Georgieva
    •  & Scott C. Blanchard

  • Article |

    Mediator is the key transcription co-activator complex that enables basal and regulated transcription initiation by RNA polymerase (Pol) II; here a 15-subunit yeast core Mediator bound to a core Pol II initiation complex is reconstituted and its structure determined by cryo-electron microscopy at subnanometre resolution.

    • C. Plaschka
    • , L. Larivière
    •  & P. Cramer

  • Letter |

    Sulfite-reducing microbes couple the reduction of sulfite to the generation of a proton motive force that sustains organismic growth; here, two X-ray crystal structures are solved of MccA, a c-type cytochrome enzyme with eight haem groups that catalyses the six-electron reduction of sulfite to sulfide at a novel haem–copper active site.

    • Bianca Hermann
    • , Melanie Kern
    •  & Oliver Einsle

  • News & Views |

    The most powerful oxidant found in nature is compound Q, an enzymatic intermediate that oxidizes methane. New spectroscopic data have resolved the long-running controversy about Q's chemical structure. See Letter p.431

    • Amy C. Rosenzweig

  • Letter |

    Time-resolved resonance Raman vibrational spectroscopy was used to study the mechanism of soluble methane monooxygenase and obtain structural information on the key reaction cycle intermediate, compound Q, which contains a unique dinuclear FeIV cluster that breaks the strong C-H bond of methane and inserts an oxygen atom (from O2) to form methanol.

    • Rahul Banerjee
    • , Yegor Proshlyakov
    •  & Denis A. Proshlyakov

  • Article |

    Using single-particle electron cryomicroscopy, several structures are reported which illuminate the mechanisms of action of the ATPase NSF that disassembles the SNARE complex into individual protein components.

    • Minglei Zhao
    • , Shenping Wu
    •  & Axel T. Brunger

  • News & Views |

    Crystal structures of the complete RNA polymerases from influenza A and B viruses provide insight into how these enzymes initiate RNA synthesis, and reveal targets for antiviral drug design. See Articles p.355 & p.361

    • Robert M. Krug

  • Article |

    Using electron cryomicroscopy, the structure of the closed-state rabbit ryanodine receptor RyR1 in complex with its modulator FKBP12 is solved at 3.8 Å; in addition to determining structural details of the ion-conducting channel domain, three previously uncharacterized domains help to reveal a molecular scaffold that allows long-range allosteric regulation of channel activities.

    • Zhen Yan
    • , Xiao-chen Bai
    •  & Nieng Yan

  • Article |

    Here the structure of the membrane protein complex sodium-translocating NADH:quinone oxidoreductase (Na+-NQR) is described; as Na+-NQR is a component of the respiratory chain of various bacteria, including pathogenic ones, this structure may serve as the basis for the development of new antibiotics.

    • Julia Steuber
    • , Georg Vohl
    •  & Günter Fritz

  • Letter |

    X-ray structures of the human TRAAK mechanosensitive potassium channel reveal how build-up of tension in the lipid membrane can convert the channel from a non-conducting wedge shape associated with an inserted lipid acyl chain that blocks the pore to an expanded cross-sectional shape that prevents lipid entry and thus permits ion conduction.

    • Stephen G. Brohawn
    • , Ernest B. Campbell
    •  & Roderick MacKinnon

  • Article |

    Using electron cryomicroscopy, the closed-state structure of rabbit RyR1 is determined at 4.8 Å resolution; analysis confirms that the RyR1 architecture consists of a six-transmembrane ion channel with a cytosolic α-solenoid scaffold, and suggests a mechanism for Ca2+-induced channel opening.

    • Ran Zalk
    • , Oliver B. Clarke
    •  & Andrew R. Marks

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