1e4v: Difference between revisions
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==Overview== | ==Overview== | ||
Two mutants of adenylate kinase from Escherichia coli have been | 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 contact that is crystallographic in one case and noncrystallographic in the other, while all other packing contacts and the space groups are quite at variance. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Mueller, C | [[Category: Mueller, C W.]] | ||
[[Category: Schulz, G | [[Category: Schulz, G E.]] | ||
[[Category: AP5]] | [[Category: AP5]] | ||
[[Category: transferase(phosphotransferase)]] | [[Category: transferase(phosphotransferase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:53 2008'' | ||
Revision as of 10:23, 21 February 2008
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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 contact that is crystallographic in one case and noncrystallographic in the other, while all other packing contacts and the space groups are quite at variance.
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 Known structural/functional 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
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