2ify

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[[Image:2ify.jpg|left|200px]]
 
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==Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase==
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The line below this paragraph, containing "STRUCTURE_2ify", creates the "Structure Box" on the page.
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<StructureSection load='2ify' size='340' side='right'caption='[[2ify]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ify]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IFY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IFY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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{{STRUCTURE_2ify| PDB=2ify | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ify FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ify OCA], [https://pdbe.org/2ify PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ify RCSB], [https://www.ebi.ac.uk/pdbsum/2ify PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ify ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GPMI_BACAN GPMI_BACAN] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/if/2ify_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ify ConSurf].
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<div style="clear:both"></div>
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'''Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase'''
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==See Also==
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*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Phosphoglycerate mutases (PGMs) catalyze the isomerization of 2- and 3-phosphoglycerates and are essential for glucose metabolism in most organisms. This study reports the production, structure, and molecular dynamics analysis of Bacillus anthracis cofactor-independent PGM (iPGM). The three-dimensional structure of B. anthracis PGM is composed of two structural and functional domains, the phosphatase and transferase. The structural relationship between these two domains is different than in the B. stearothermophilus iPGM structure determined previously. However, the structures of the two domains of B. anthracis iPGM show a high degree of similarity to those in B. stearothermophilus iPGM. The novel domain arrangement in B. anthracis iPGM and the dynamic property of these domains is directly linked to the mechanism of enzyme catalysis, in which substrate binding is proposed to result in close association of the two domains. The structure of B. anthracis iPGM and the molecular dynamics of this structure provide unique insight into the mechanism of iPGM catalysis, in particular the roles of changes in coordination geometry of the enzyme's two bivalent metal ions and the regulation of this enzyme's activity by changes in intracellular pH during spore formation and germination in Bacillus species.
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==About this Structure==
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2IFY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IFY OCA].
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==Reference==
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Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species., Nukui M, Mello LV, Littlejohn JE, Setlow B, Setlow P, Kim K, Leighton T, Jedrzejas MJ, Biophys J. 2007 Feb 1;92(3):977-88. Epub 2006 Nov 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17085493 17085493]
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[[Category: Bacillus anthracis]]
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[[Category: Phosphoglycerate mutase]]
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[[Category: Single protein]]
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[[Category: Jedrzejas, M J.]]
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[[Category: Littlejohn, J E.]]
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[[Category: Nukui, M.]]
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[[Category: Bacillus anthracis]]
[[Category: Bacillus anthracis]]
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[[Category: Catalysis]]
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[[Category: Large Structures]]
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[[Category: Catalytic mechanism]]
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[[Category: Jedrzejas MJ]]
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[[Category: Glygolysis]]
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[[Category: Littlejohn JE]]
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[[Category: Gram-posotive bacteria]]
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[[Category: Nukui M]]
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[[Category: Phosphoglycerate]]
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[[Category: Spore]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:27:30 2008''
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Current revision

Structure of Bacillus anthracis cofactor-independent phosphoglucerate mutase

PDB ID 2ify

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