1g99: Difference between revisions
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<StructureSection load='1g99' size='340' side='right' caption='[[1g99]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1g99' size='340' side='right' caption='[[1g99]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1g99]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1g99]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_1825 Dsm 1825]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G99 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2210 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2210 DSM 1825])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate_kinase Acetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.1 2.7.2.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetate_kinase Acetate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.1 2.7.2.1] </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=1g99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g99 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g99 RCSB], [http://www.ebi.ac.uk/pdbsum/1g99 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=1g99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g99 OCA], [http://pdbe.org/1g99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g99 RCSB], [http://www.ebi.ac.uk/pdbsum/1g99 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1g99" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Acetate kinase]] | [[Category: Acetate kinase]] | ||
[[Category: | [[Category: Dsm 1825]] | ||
[[Category: Buss, K A]] | [[Category: Buss, K A]] | ||
[[Category: Cooper, D R]] | [[Category: Cooper, D R]] | ||
Revision as of 06:52, 10 September 2015
AN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILAAN ANCIENT ENZYME: ACETATE KINASE FROM METHANOSARCINA THERMOPHILA
Structural highlights
Function[ACKA_METTE] Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Can also phosphorylate propionate, but has very low activity toward butyrate.[1] 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 PubMedAcetate kinase, an enzyme widely distributed in the Bacteria and Archaea domains, catalyzes the phosphorylation of acetate. We have determined the three-dimensional structure of Methanosarcina thermophila acetate kinase bound to ADP through crystallography. As we previously predicted, acetate kinase contains a core fold that is topologically identical to that of the ADP-binding domains of glycerol kinase, hexokinase, the 70-kDa heat shock cognate (Hsc70), and actin. Numerous charged active-site residues are conserved within acetate kinases, but few are conserved within the phosphotransferase superfamily. The identity of the points of insertion of polypeptide segments into the core fold of the superfamily members indicates that the insertions existed in the common ancestor of the phosphotransferases. Another remarkable shared feature is the unusual, epsilon conformation of the residue that directly precedes a conserved glycine residue (Gly-331 in acetate kinase) that binds the alpha-phosphate of ADP. Structural, biochemical, and geochemical considerations indicate that an acetate kinase may be the ancestral enzyme of the ASKHA (acetate and sugar kinases/Hsc70/actin) superfamily of phosphotransferases. Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases.,Buss KA, Cooper DR, Ingram-Smith C, Ferry JG, Sanders DA, Hasson MS J Bacteriol. 2001 Jan;183(2):680-6. PMID:11133963[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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