3lnt: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3lnt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LNT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LNT FirstGlance]. <br> | <table><tr><td colspan='2'>[[3lnt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LNT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LNT FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gw8|3gw8]], [[3gp3|3gp3]], [[3gp5|3gp5]], [[3fdz|3fdz]], [[3ezn|3ezn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gw8|3gw8]], [[3gp3|3gp3]], [[3gp5|3gp5]], [[3fdz|3fdz]], [[3ezn|3ezn]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gpmA, BURPS1710b_0662 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 Burkholderia pseudomallei])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gpmA, BURPS1710b_0662 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 Burkholderia pseudomallei])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lnt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lnt RCSB], [http://www.ebi.ac.uk/pdbsum/3lnt 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=3lnt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lnt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lnt RCSB], [http://www.ebi.ac.uk/pdbsum/3lnt PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/GPMA_BURP1 GPMA_BURP1]] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).[HAMAP-Rule:MF_01039] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Burkholderia pseudomallei]] | [[Category: Burkholderia pseudomallei]] | ||
[[Category: Phosphoglycerate mutase]] | [[Category: Phosphoglycerate mutase]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Glycolysis]] | [[Category: Glycolysis]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Mutase]] | [[Category: Mutase]] | ||
[[Category: Phosphoglycerylmutase]] | [[Category: Phosphoglycerylmutase]] | ||
[[Category: Ssgcid]] | [[Category: Ssgcid]] | ||
Revision as of 01:36, 26 December 2014
Crystal structure of phosphoglyceromutase from Burkholderia Pseudomallei 1710B with bound malonic acidCrystal structure of phosphoglyceromutase from Burkholderia Pseudomallei 1710B with bound malonic acid
Structural highlights
Function[GPMA_BURP1] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).[HAMAP-Rule:MF_01039] 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 PubMedBurkholderia pseudomallei is a soil-dwelling bacterium endemic to Southeast Asia and Northern Australia. Burkholderia is responsible for melioidosis, a serious infection of the skin. The enzyme 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (PGAM) catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate, a key step in the glycolytic pathway. As such it is an extensively studied enzyme and X-ray crystal structures of PGAM enzymes from multiple species have been elucidated. Vanadate is a phosphate mimic that is a powerful tool for studying enzymatic mechanisms in phosphoryl-transfer enzymes such as phosphoglycerate mutase. However, to date no X-ray crystal structures of phosphoglycerate mutase have been solved with vanadate acting as a substrate mimic. Here, two vanadate complexes together with an ensemble of substrate and fragment-bound structures that provide a comprehensive picture of the function of the Burkholderia enzyme are reported. An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase.,Davies DR, Staker BL, Abendroth JA, Edwards TE, Hartley R, Leonard J, Kim H, Rychel AL, Hewitt SN, Myler PJ, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1044-50. Epub 2011 Aug 13. PMID:21904048[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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