Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1e4v
From Proteopedia
| Line 20: | Line 20: | ||
[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10: | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:04:28 2007'' |
Revision as of 07:59, 30 October 2007
|
MUTANT G10V OF ADENYLATE KINASE FROM E. COLI, MODIFIED IN THE GLY-LOOP
Overview
Two mutants of adenylate kinase from Escherichia coli have been, crystallized and analyzed by X-ray diffraction at resolutions of 3.4 and, 2.4 A, respectively. These mutants are Pro-9-->Leu and Gly-10-->Val. They, were selected for their positions in the highly conserved Gly-loop forming, a giant anion hole for the beta-phosphate of ATP (GTP) in adenylate, kinases, H-ras-p21, and other nucleotide-binding proteins. Mutants at, these positions of H-ras-p21 cause cancer. In adenylate kinase these, mutations cause smallish changes at the active site. Relating the, structural changes to the known changes in catalysis indicates that these, mutants hinder the induced-fit movements. As a side result we find that, mutant Pro-9-->Leu and wild-type form one very similar crystal packing, ... [(full description)]
About this Structure
1E4V is a [Single protein] structure of sequence from [Escherichia coli] with AP5 as [ligand]. Active as [Adenylate kinase], with EC number [2.7.4.3]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [OCA].
Reference
Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop., Muller CW, Schulz GE, Proteins. 1993 Jan;15(1):42-9. PMID:8451239
Page seeded by OCA on Tue Oct 30 10:04:28 2007
