1e4v: Difference between revisions
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==Mutant G10V of adenylate kinase from E. coli, modified in the Gly-loop== | |||
<StructureSection load='1e4v' size='340' side='right' caption='[[1e4v]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='1e4v' size='340' side='right' caption='[[1e4v]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ake|4ake]], [[2eck|2eck]], [[1ake|1ake]], [[1ank|1ank]], [[1e4y|1e4y]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ake|4ake]], [[2eck|2eck]], [[1ake|1ake]], [[1ank|1ank]], [[1e4y|1e4y]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4v OCA], [http://pdbe.org/1e4v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e4v RCSB], [http://www.ebi.ac.uk/pdbsum/1e4v PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4v OCA], [http://pdbe.org/1e4v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e4v RCSB], [http://www.ebi.ac.uk/pdbsum/1e4v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1e4v" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1e4v" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:56, 16 November 2017
Mutant G10V of adenylate kinase from E. coli, modified in the Gly-loopMutant G10V of adenylate kinase from E. coli, modified in the Gly-loop
Structural highlights
Function[KAD_ECOLI] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth.[HAMAP-Rule:MF_00235] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTwo 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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