Looking ahead with structural genomics - p1

doi:10.1038/nsmb0107-1

Abstract - Looking ahead with structural genomics | Full Text - Looking ahead with structural genomics | PDF (78 KB) - Looking ahead with structural genomics

Natalia Sergeevna Andreeva 1922–2006 - p2

Alexander Wlodawer

doi:10.1038/nsmb0107-2

Full Text - Natalia Sergeevna Andreeva 1922–2006 | PDF (129 KB) - Natalia Sergeevna Andreeva 1922–2006

Structural proteomics: from the molecule to the system - pp3 - 4

Lucia Banci, Wolfgang Baumeister, Josefina Enfedaque, Udo Heinemann, Gunter Schneider, Israel Silman & Joel L Sussman

doi:10.1038/nsmb0107-3

Full Text - Structural proteomics: from the molecule to the system | PDF (69 KB) - Structural proteomics: from the molecule to the system

Wrong PH for RNA degradation - pp5 - 7

Elmar Wahle

doi:10.1038/nsmb0107-5

Full Text - Wrong PH for RNA degradation | PDF (502 KB) - Wrong PH for RNA degradation

See also: Article by Dziembowski et al.

Insights into DNA deaminases - pp7 - 9

Silvestro G Conticello, Marc-Andre Langlois & Michael S Neuberger

doi:10.1038/nsmb0107-7

Full Text - Insights into DNA deaminases | PDF (2,452 KB) - Insights into DNA deaminases

Botulinum neurotoxin B–host receptor recognition: it takes two receptors to tango - pp9 - 10

Michael R Baldwin, Jung-Ja P Kim & Joseph T Barbieri

doi:10.1038/nsmb0107-9

Full Text - Botulinum neurotoxin B–host receptor recognition: it takes two receptors to tango | PDF (2,304 KB) - Botulinum neurotoxin B–host receptor recognition: it takes two receptors to tango

A Hec of a microtubule attachment - pp11 - 13

Michael Emanuele, Daniel J Burke & P Todd Stukenberg

doi:10.1038/nsmb0107-11

Full Text - A Hec of a microtubule attachment | PDF (609 KB) - A Hec of a microtubule attachment

See also: Article by Wei et al.

All mixed up - p13

Angela K Eggleston

doi:10.1038/nsmb0107-13

Full Text - All mixed up | PDF (240 KB) - All mixed up

Research Highlights - p14

doi:10.1038/nsmb0107-14

Full Text - Research Highlights | PDF (143 KB) - Research Highlights

A single subunit, Dis3, is essentially responsible for yeast exosome core activity - pp15 - 22

Andrzej Dziembowski, Esben Lorentzen, Elena Conti & Bertrand Séraphin

doi:10.1038/nsmb1184

Abstract - A single subunit, Dis3, is essentially responsible for yeast exosome core activity | Full Text - A single subunit, Dis3, is essentially responsible for yeast exosome core activity | PDF (430 KB) - A single subunit, Dis3, is essentially responsible for yeast exosome core activity | Supplementary information

See also: News and Views by Wahle

Heme is involved in microRNA processing - pp23 - 29

Michael Faller, Michio Matsunaga, Sheng Yin, Joseph A Loo & Feng Guo

doi:10.1038/nsmb1182

Abstract - Heme is involved in microRNA processing | Full Text - Heme is involved in microRNA processing | PDF (394 KB) - Heme is involved in microRNA processing | Supplementary information

Mutational analysis reveals two independent molecular requirements during transfer RNA selection on the ribosome - pp30 - 36

Luisa Cochella, Julie L Brunelle & Rachel Green

doi:10.1038/nsmb1183

Abstract - Mutational analysis reveals two independent molecular requirements during transfer RNA selection on the ribosome | Full Text - Mutational analysis reveals two independent molecular requirements during transfer RNA selection on the ribosome | PDF (283 KB) - Mutational analysis reveals two independent molecular requirements during transfer RNA selection on the ribosome | Supplementary information

A folding control element for tertiary collapse of a group II intron ribozyme - pp37 - 44

Christina Waldsich & Anna Marie Pyle

doi:10.1038/nsmb1181

Abstract - A folding control element for tertiary collapse of a group II intron ribozyme | Full Text - A folding control element for tertiary collapse of a group II intron ribozyme | PDF (561 KB) - A folding control element for tertiary collapse of a group II intron ribozyme | Supplementary information

Structural insight into the substrate specificity of DNA Polymerase - pp45 - 53

Andrea F Moon, Miguel Garcia-Diaz, Katarzyna Bebenek, Bryan J Davis, Xuejun Zhong, Dale A Ramsden, Thomas A Kunkel & Lars C Pedersen

doi:10.1038/nsmb1180

• PDB code

  • 2IHM

• 3D view

  • 2IHM

Abstract - Structural insight into the substrate specificity of DNA Polymerase [mu] | Full Text - Structural insight into the substrate specificity of DNA Polymerase | PDF (950 KB) - Structural insight into the substrate specificity of DNA Polymerase

The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment - pp54 - 59

Ronnie R Wei, Jawdat Al-Bassam & Stephen C Harrison

doi:10.1038/nsmb1186

• PDB code

  • 2IGP

• 3D view

  • 2IGP

Abstract - The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment | Full Text - The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment | PDF (532 KB) - The Ndc80/HEC1 complex is a contact point for kinetochore-microtubule attachment | Supplementary information

See also: News and Views by Emanuele et al.

Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5 - pp60 - 67

Sebastian Meyer, Sara Savaresi, Ian C Forster & Raimund Dutzler

doi:10.1038/nsmb1188

• PDB code

  • 2J9L
  • 2JA3

• 3D view

  • 2J9L
  • 2JA3

Abstract - Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5 | Full Text - Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5 | PDF (645 KB) - Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5 | Supplementary information

SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells - pp68 - 75

Sung Wook Park, Xinli Hu, Pawan Gupta, Ya-Ping Lin, Sung Gil Ha & Li-Na Wei

doi:10.1038/nsmb1185

Abstract - SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells | Full Text - SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells | PDF (441 KB) - SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells

Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors - pp76 - 84

Alicia Lammerts van Bueren, Melanie Higgins, Diana Wang, Robert D Burke & Alisdair B Boraston

doi:10.1038/nsmb1187

• PDB code

  • 2J43
  • 2J44

• 3D view

  • 2J43
  • 2J44

Abstract - Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors | Full Text - Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors | PDF (658 KB) - Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors

An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane - pp85 - 87

Trevor F Moraes, Manjeet Bains, Robert E W Hancock & Natalie C J Strynadka

doi:10.1038/nsmb1189

• PDB code

  • 2O4V

• 3D view

  • 2O4V

Abstract - An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane | Full Text - An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane | PDF (307 KB) - An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane | Supplementary information