1k35
From Proteopedia
(Difference between revisions)
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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=1k35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k35 OCA], [https://pdbe.org/1k35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k35 RCSB], [https://www.ebi.ac.uk/pdbsum/1k35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k35 ProSAT]</span></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=1k35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k35 OCA], [https://pdbe.org/1k35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k35 RCSB], [https://www.ebi.ac.uk/pdbsum/1k35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k35 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k35_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k3/1k35_consurf.spt"</scriptWhenChecked> | ||
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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=1k35 ConSurf]. | </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=1k35 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from P. aeruginosa is required for the biosynthesis of two bacterial exopolysaccharides: alginate and lipopolysaccharide (LPS). Both of these molecules play a role in the virulence of P. aeruginosa, an important human pathogen known for its ability to develop antibiotic resistance and cause chronic lung infections in cystic fibrosis patients. The crystal structure of PMM/PGM shows that the enzyme has four domains, three of which have a similar three-dimensional fold. Residues from all four domains of the protein contribute to the formation of a large active site cleft in the center of the molecule. Detailed information on the active site of PMM/PGM lays the foundation for structure-based inhibitor design. Inhibitors of sufficient potency and specificity should impair the biosynthesis of alginate and LPS, and may facilitate clearance of the bacteria by the host immune system and increase the efficacy of conventional antibiotic treatment against chronic P. aeruginosa infections. | ||
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| + | Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.,Regni C, Tipton PA, Beamer LJ Structure. 2002 Feb;10(2):269-79. PMID:11839312<ref>PMID:11839312</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1k35" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa
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