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3bkq

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Revision as of 07:38, 31 October 2018

Structure of the P368G mutant of PMM/PGM in complex with its substrate

Structural highlights

3bkq is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1p5d, 1k2y, 1p5g, 1k35
Gene:	algC (Pseudomonas aeruginosa)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Coyne MJ Jr, Russell KS, Coyle CL, Goldberg JB. The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core. J Bacteriol. 1994 Jun;176(12):3500-7. PMID:7515870
↑ Olvera C, Goldberg JB, Sanchez R, Soberon-Chavez G. The Pseudomonas aeruginosa algC gene product participates in rhamnolipid biosynthesis. FEMS Microbiol Lett. 1999 Oct 1;179(1):85-90. PMID:10481091
↑ Schramm AM, Mehra-Chaudhary R, Furdui CM, Beamer LJ. Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa. Biochemistry. 2008 Sep 2;47(35):9154-62. Epub 2008 Aug 9. PMID:18690721 doi:http://dx.doi.org/10.1021/bi8005219

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bkq"

@@ Line 1: / Line 1: @@
 ==Structure of the P368G mutant of PMM/PGM in complex with its substrate==
 <StructureSection load='3bkq' size='340' side='right' caption='[[3bkq]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p5d|1p5d]], [[1k2y|1k2y]], [[1p5g|1p5g]], [[1k35|1k35]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">algC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bkq OCA], [http://pdbe.org/3bkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bkq RCSB], [http://www.ebi.ac.uk/pdbsum/3bkq PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bkq OCA], [http://pdbe.org/3bkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bkq RCSB], [http://www.ebi.ac.uk/pdbsum/3bkq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bkq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/3bkq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/3bkq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3bkq

From Proteopedia

Revision as of 07:38, 31 October 2018

Structure of the P368G mutant of PMM/PGM in complex with its substrate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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