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| {{STRUCTURE_1e4y| PDB=1e4y | SCENE= }} | | {{STRUCTURE_1e4y| PDB=1e4y | SCENE= }} |
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| '''MUTANT P9L OF ADENYLATE KINASE FROM E. COLI, MODIFIED IN THE GLY-LOOP'''
| | ===MUTANT P9L OF ADENYLATE KINASE FROM E. COLI, MODIFIED IN THE GLY-LOOP=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_8451239}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8451239 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8451239}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Mueller, C W.]] | | [[Category: Mueller, C W.]] |
| [[Category: Schulz, G E.]] | | [[Category: Schulz, G E.]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:40:02 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:09:26 2008'' |