Holoenzymes articles within Nature

Featured

• Article | 07 September 2022

  Structure of dynein–dynactin on microtubules shows tandem adaptor binding

  The structure of the complete dynein–dynactin complex and its interaction with microtubules and cargo adaptors are visualized using cryo-electron microscopy.

  • Sami Chaaban
  •  & Andrew P. Carter

• Article | 08 July 2020

  Structures of fungal and plant acetohydroxyacid synthases

  Structures of the acetohydroxyacid synthase complexes of Saccharomyces cerevisiae and Arabidopsis thaliana provide insights into the biosynthesis of and feedback inhibition by branched-chain amino acids.

  • Thierry Lonhienne
  • , Yu Shang Low
  •  & Luke W. Guddat

• Article | 16 July 2014

  Crystal structure of the human COP9 signalosome

  The COP9 signalosome (CSN) complex regulates cullin–RING E3 ubiquitin ligases—the largest class of ubiquitin ligase enzymes, which are involved in a multitude of regulatory processes; here, the crystal structure of the entire human CSN holoenzyme is presented.

  • Gondichatnahalli M. Lingaraju
  • , Richard D. Bunker
  •  & Nicolas H. Thomä

• Letter | 11 December 2011

  An unanticipated architecture of the 750-kDa α₆β₆ holoenzyme of 3-methylcrotonyl-CoA carboxylase

  The crystal structure of Pseudomonas aeruginosa 3-methylcrotonyl-CoA carboxylase is determined and found to be markedly different from that of propionyl-CoA carboxylase.

  • Christine S. Huang
  • , Peng Ge
  •  & Liang Tong

• Article | 14 November 2010

  Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA

  tRNAs are synthesized in a premature form that requires trimming of the 5′ and 3′ ends and modification of specific nucleotides. RNase P, a complex containing a long catalytic RNA and a protein cofactor, catalyses the cleavage that generates the mature 5′ end. Here, the structure of RNase P bound to mature tRNA^Phe is solved. Recognition of the leader sequence and its mechanism of cleavage is determined by soaking an oligonucleotide corresponding to the premature 5′ end into the crystal.

  • Nicholas J. Reiter
  • , Amy Osterman
  •  & Alfonso Mondragón

• Letter | 19 August 2010

  Crystal structure of the α₆β₆ holoenzyme of propionyl-coenzyme A carboxylase

  Propionyl-coenzyme A carboxylase (PCC) is a biotin-dependent enzyme that is essential for the catabolism of several amino acids, cholesterol and some fatty acids. Here, the crystal structure of a bacterial PCC is presented, along with a cryo-electron microscopy reconstruction showing a similar structure for human PCC. The structural information establishes a molecular basis for understanding the known disease-causing mutations in PCC, and is relevant to the holoenzymes of other biotin-dependent carboxylases.

  • Christine S. Huang
  • , Kianoush Sadre-Bazzaz
  •  & Liang Tong