2wfp

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{{Seed}}
 
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[[Image:2wfp.jpg|left|200px]]
 
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==Crystal structure of mannose 6-phosphate isomerase (apo form) from Salmonella typhimurium==
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The line below this paragraph, containing "STRUCTURE_2wfp", creates the "Structure Box" on the page.
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<StructureSection load='2wfp' size='340' side='right'caption='[[2wfp]], [[Resolution|resolution]] 1.67&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'>[[2wfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFP 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]] 1.67&#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=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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{{STRUCTURE_2wfp| PDB=2wfp | 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=2wfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfp OCA], [https://pdbe.org/2wfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wfp RCSB], [https://www.ebi.ac.uk/pdbsum/2wfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MANA_SALTY MANA_SALTY] Involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide.
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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/wf/2wfp_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=2wfp ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mannose-6-phosphate isomerase (MPI) catalyzes the interconversion of mannose 6-phosphate and fructose 6-phosphate. X-ray crystal structures of MPI from Salmonella typhimurium in the apo form (with no metal bound) and in the holo form (with bound Zn2+) and two other structures with yttrium bound at an inhibitory site and complexed with Zn2+ and fructose 6-phosphate (F6P) were determined in order to gain insights into the structure and the isomerization mechanism. Isomerization involves acid/base catalysis with proton transfer between the C1 and C2 atoms of the substrate. His99, Lys132, His131 and Asp270 are close to the substrate and are likely to be the residues involved in proton transfer. The interactions observed at the active site suggest that the ring-opening step is probably catalyzed by His99 and Asp270. An active-site loop consisting of residues 130-133 undergoes conformational changes upon substrate binding. Zn2+ binding induces structural order in the loop consisting of residues 50-54. The metal atom appears to play a role in substrate binding and is probably also important for maintaining the architecture of the active site. Isomerization probably follows the previously suggested cis-enediol mechanism.
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===CRYSTAL STRUCTURE OF MANNOSE 6-PHOSPHATE ISOMERASE (APO FORM) FROM SALMONELLA TYPHIMURIUM===
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Structures of mannose-6-phosphate isomerase from Salmonella typhimurium bound to metal atoms and substrate: implications for catalytic mechanism.,Sagurthi SR, Gowda G, Savithri HS, Murthy MR Acta Crystallogr D Biol Crystallogr. 2009 Jul;65(Pt 7):724-32. Epub 2009, Jun 20. PMID:19564693<ref>PMID:19564693</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19564693}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2wfp" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19564693 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19564693}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2WFP is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFP OCA].
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
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[[Category: Sagurthi SR]]
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==Reference==
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<ref group="xtra">PMID:19564693</ref><references group="xtra"/>
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[[Category: Mannose-6-phosphate isomerase]]
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[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
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[[Category: Sagurthi, S R.]]
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[[Category: Apo-structure]]
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[[Category: Cytoplasm]]
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[[Category: Isomerase]]
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[[Category: Metal-binding]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 15 08:42:58 2009''
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Current revision

Crystal structure of mannose 6-phosphate isomerase (apo form) from Salmonella typhimurium

PDB ID 2wfp

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