2aak
UBIQUITIN CONJUGATING ENZYME FROM ARABIDOPSIS THALIANA
OverviewOverview
The x-ray crystal structure of a recombinant ubiquitin-conjugating enzyme (E2) encoded by the UBC1 gene of the plant Arabidopsis thaliana has been determined with the use of multiple isomorphous replacement techniques and refined at 2.4-A resolution by simulated annealing and restrained least-squares. This E2 is an alpha/beta protein, with four alpha-helices and a four-stranded antiparallel beta-sheet. The NH2 and COOH termini, which may be important for interaction with other enzymes and substrates in the ubiquitin-conjugation pathway, are on the opposite side of the molecule from the cysteine residue that binds to the COOH terminus of ubiquitin. This structure should now allow for the rational analysis of E2 function by in vitro mutagenesis and facilitate the effective design of E2s with unique specificities or catalytic functions.
About this StructureAbout this Structure
2AAK is a Single protein structure of sequence from Arabidopsis thaliana. This structure supersedes the now removed PDB entry 1aak. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of a ubiquitin-conjugating enzyme (E2)., Cook WJ, Jeffrey LC, Sullivan ML, Vierstra RD, J Biol Chem. 1992 Jul 25;267(21):15116-21. PMID:1321826 Page seeded by OCA on Sat May 3 18:49:06 2008