2UCZ

UBIQUITIN CONJUGATING ENZYME (UBC7) FROM SACCHAROMYCES CEREVISIAE

「1UCZ」から置き換えられました

2UCZ の概要

• エントリーDOI: 10.2210/pdb2ucz/pdb
• 分子名称: UBIQUITIN CONJUGATING ENZYME (1 entity in total)
• 機能のキーワード: ubiquitin conjugation, ligase, yeast
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side: Q02159
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18538.27

構造登録者

Cook, W.J.,Chau, V. (登録日: 1997-11-07, 公開日: 1998-03-18, 最終更新日: 2024-05-22)

主引用文献

Cook, W.J.,Martin, P.D.,Edwards, B.F.,Yamazaki, R.K.,Chau, V.
Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9 angstroms resolution.
Biochemistry, 36:1621-1627, 1997

PubMed Abstract: Ubiquitin-conjugating enzymes are a family of related proteins that participate in the ubiquitination of proteins. Previous studies on the crystal structures of Saccharomyces cerevisiae Ubc4 and Arabidopsis thaliana Ubc1 indicated that the smallest enzymes (class I), which consist entirely of the conserved core domain, share a common tertiary fold. Here we report the three-dimensional structure of the S. cerevisiae class I enzyme encoded by the UBC7 gene. The crystal structure has been solved using molecular replacement techniques and refined by simulated annealing to an R-factor of 0.183 at 2.93 A resolution. Bond lengths and angles in the molecule have root-mean-square deviations from ideal values of 0.016 A and 2.3 degrees, respectively. Ubc7 is an alpha/beta protein with four alpha-helices and a four-stranded antiparallel beta-sheet. With the exception of two regions where extra residues are present, the tertiary folding of Ubc7 is similar to those of the other two enzymes. The ubiquitin-accepting cysteine is located in a cleft between two loops. One of these loops is nonconserved, as this region of the Ubc7 molecule differs from the other two enzymes by having 13 extra residues. There is also a second single amino acid insertion that alters the orientation of the turn between the first two beta-strands. Analysis of the 13 ubiquitin-conjugating enzyme sequences in S. cerevisiae indicates that there may be two other regions where extra residues could be inserted into the common tertiary fold. Both of these other regions exhibit significant deviations in the superposition of the three structures and, like the two insertion regions in Ubc7, may represent hypervariable regions within a common tertiary fold. As ubiquitin-conjugating enzymes interact with different substrates or other accessory proteins in the ubiquitination pathway, these variable surface regions may confer distinct specificity to individual enzymes.

PubMed: 9048545
DOI: 10.1021/bi962639e

実験手法

X-RAY DIFFRACTION (2.93 Å)