1rii: Difference between revisions
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<StructureSection load='1rii' size='340' side='right'caption='[[1rii]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1rii' size='340' side='right'caption='[[1rii]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1rii]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1rii]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RII FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rii OCA], [https://pdbe.org/1rii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rii RCSB], [https://www.ebi.ac.uk/pdbsum/1rii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rii ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GPMA_MYCTU GPMA_MYCTU] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Chan | [[Category: Chan S]] | ||
[[Category: Eisenberg | [[Category: Eisenberg D]] | ||
[[Category: Mueller | [[Category: Mueller P]] | ||
[[Category: Pashkova | [[Category: Pashkova I]] | ||
[[Category: Perry | [[Category: Perry J]] | ||
[[Category: Sawaya | [[Category: Sawaya MR]] | ||
[[Category: Wu Y]] | |||
[[Category: Wu | |||
Latest revision as of 09:04, 23 August 2023
Crystal structure of phosphoglycerate mutase from M. TuberculosisCrystal structure of phosphoglycerate mutase from M. Tuberculosis
Structural highlights
FunctionGPMA_MYCTU Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity). 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 PubMedThe single-crystal X-ray structure of phosphoglycerate mutase from Mycobacterium tuberculosis has been determined at a resolution of 1.70 angstroms. The C-terminal tail of each of the subunits is flexible and disordered; however, for one of the four chains (chain A) all but five residues of the chain could be modeled. Noteworthy features of the structure include the active site and a proline-rich segment in each monomer forming a short left-handed polyprolyl helix. These segments lie on the enzyme surface and could conceivably participate in protein-protein interactions. The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.,Muller P, Sawaya MR, Pashkov I, Chan S, Nguyen C, Wu Y, Perry LJ, Eisenberg D Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):309-15. Epub 2005, Feb 24. PMID:15735341[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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