3c04

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{{Seed}}
 
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[[Image:3c04.png|left|200px]]
 
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==Structure of the P368G mutant of PMM/PGM from P. aeruginosa==
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The line below this paragraph, containing "STRUCTURE_3c04", creates the "Structure Box" on the page.
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<StructureSection load='3c04' size='340' side='right'caption='[[3c04]], [[Resolution|resolution]] 2.20&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'>[[3c04]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C04 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]] 2.2&#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=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3c04| PDB=3c04 | 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=3c04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c04 OCA], [https://pdbe.org/3c04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c04 RCSB], [https://www.ebi.ac.uk/pdbsum/3c04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c04 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/c0/3c04_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=3c04 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 the bacterium Pseudomonas aeruginosa is involved in the biosynthesis of several complex carbohydrates, including alginate, lipopolysaccharide, and rhamnolipid. Previous structural studies of this protein have shown that binding of substrates produces a rotation of the C-terminal domain, changing the active site from an open cleft in the apoenzyme into a deep, solvent inaccessible pocket where phosphoryl transfer takes place. We report herein site-directed mutagenesis, kinetic, and structural studies in examining the role of residues in the hinge between domains 3 and 4, as well as residues that participate in enzyme-substrate contacts and help form the multidomain "lid" of the active site. We find that the backbone flexibility of residues in the hinge region (e.g., mutation of proline to glycine/alanine) affects the efficiency of the reaction, decreasing k cat by approximately 10-fold and increasing K m by approximately 2-fold. Moreover, thermodynamic analyses show that these changes are due primarily to entropic effects, consistent with an increase in the flexibility of the polypeptide backbone leading to a decreased probability of forming a catalytically productive active site. These results for the hinge residues contrast with those for mutants in the active site of the enzyme, which have profound effects on enzyme kinetics (10 (2)-10 (3)-fold decrease in k cat/ K m) and also show substantial differences in their thermodynamic parameters relative to those of the wild-type (WT) enzyme. These studies support the concept that polypeptide flexibility in protein hinges may evolve to optimize and tune reaction rates.
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===Structure of the P368G mutant of PMM/PGM from P. aeruginosa===
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Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa.,Schramm AM, Mehra-Chaudhary R, Furdui CM, Beamer LJ Biochemistry. 2008 Sep 2;47(35):9154-62. Epub 2008 Aug 9. PMID:18690721<ref>PMID:18690721</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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<div class="pdbe-citations 3c04" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18690721}}, adds the Publication Abstract to the page
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*[[Phosphomannomutase|Phosphomannomutase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18690721 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18690721}}
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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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3C04 is a 1 chain structure of 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=3C04 OCA].
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Beamer LJ]]
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==Reference==
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[[Category: Mehra-Chaudhary R]]
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<ref group="xtra">PMID:18690721</ref><references group="xtra"/>
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Beamer, L J.]]
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[[Category: Mehra-Chaudhary, R.]]
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[[Category: Alginate biosynthesis]]
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[[Category: Enzyme]]
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[[Category: Isomerase]]
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[[Category: Lipopolysaccharide biosynthesis]]
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[[Category: Magnesium]]
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[[Category: Metal-binding]]
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[[Category: Multifunctional enzyme]]
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[[Category: Mutant]]
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[[Category: Phosphoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:26:58 2009''
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Current revision

Structure of the P368G mutant of PMM/PGM from P. aeruginosa

PDB ID 3c04

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