2ucz

From Proteopedia

Revision as of 15:32, 30 October 2007

UBIQUITIN CONJUGATING ENZYME (UBC7) FROM SACCHAROMYCES CEREVISIAE

Overview

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 ... [(full description)]

About this Structure

2UCZ is a [Single protein] structure of sequence from [Saccharomyces cerevisiae]. This structure superseeds the now removed PDB entry 1UCZ. Active as [Ubiquitin--protein ligase], with EC number [6.3.2.19]. Structure known Active Site: C89. Full crystallographic information is available from [OCA].

Reference

Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9 angstroms resolution., Cook WJ, Martin PD, Edwards BF, Yamazaki RK, Chau V, Biochemistry. 1997 Feb 18;36(7):1621-7. PMID:9048545

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