2fkm

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[[Image:2fkm.png|left|200px]]
 
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{{STRUCTURE_2fkm| PDB=2fkm | SCENE= }}
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==PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound==
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<StructureSection load='2fkm' size='340' side='right'caption='[[2fkm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fkm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FKM FirstGlance]. <br>
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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]] 1.9&#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=G16:ALPHA-D-GLUCOSE+1,6-BISPHOSPHATE'>G16</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=2fkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fkm OCA], [https://pdbe.org/2fkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fkm RCSB], [https://www.ebi.ac.uk/pdbsum/2fkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fkm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ALGC_PSEAE ALGC_PSEAE] The phosphomannomutase activity produces a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core-LPS biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity, and for biofilm production.<ref>PMID:7515870</ref> <ref>PMID:10481091</ref>
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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/fk/2fkm_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=2fkm 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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The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars. The reaction entails two phosphoryl transfers, with an intervening 180 degrees reorientation of the reaction intermediate (e.g. glucose 1,6-bisphosphate) during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is, thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Structural characterization of two PMM/PGM-intermediate complexes with glucose 1,6-bisphosphate provides new insights into the reaction catalyzed by the enzyme, including the reorientation of the intermediate. Kinetic analyses of site-directed mutants prompted by the structural studies reveal active site residues critical for maintaining association with glucose 1,6-bisphosphate during its unique dynamic reorientation in the active site of PMM/PGM.
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===PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound===
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The reaction of phosphohexomutase from Pseudomonas aeruginosa: structural insights into a simple processive enzyme.,Regni C, Schramm AM, Beamer LJ J Biol Chem. 2006 Jun 2;281(22):15564-71. Epub 2006 Apr 4. PMID:16595672<ref>PMID:16595672</ref>
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{{ABSTRACT_PUBMED_16595672}}
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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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==About this Structure==
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<div class="pdbe-citations 2fkm" style="background-color:#fffaf0;"></div>
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[[2fkm]] is a 1 chain structure of [[Phosphomannomutase]] with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKM OCA].
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==See Also==
==See Also==
*[[Phosphomannomutase|Phosphomannomutase]]
*[[Phosphomannomutase|Phosphomannomutase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:016595672</ref><references group="xtra"/>
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__TOC__
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[[Category: Phosphomannomutase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Beamer, L J.]]
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[[Category: Beamer LJ]]
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[[Category: Regni, C A.]]
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[[Category: Regni CA]]
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[[Category: Alpha/beta protein]]
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[[Category: Enzyme-ligand complex]]
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[[Category: Enzyme-metal complex]]
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[[Category: Isomerase]]
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Current revision

PMM/PGM S108D mutant with alpha-d-glucose 1,6-bisphosphate bound

PDB ID 2fkm

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