2h5a: Difference between revisions

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==Complex of the enzyme PMM/PGM with xylose 1-phosphate==
==Complex of the enzyme PMM/PGM with xylose 1-phosphate==
<StructureSection load='2h5a' size='340' side='right' caption='[[2h5a]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
<StructureSection load='2h5a' size='340' side='right' caption='[[2h5a]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k35|1k35]], [[1k2y|1k2y]], [[1p5d|1p5d]], [[1p5g|1p5g]], [[1pcj|1pcj]], [[1pcm|1pcm]], [[2h4l|2h4l]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k35|1k35]], [[1k2y|1k2y]], [[1p5d|1p5d]], [[1p5g|1p5g]], [[1pcj|1pcj]], [[1pcm|1pcm]], [[2h4l|2h4l]]</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 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=2h5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5a OCA], [http://pdbe.org/2h5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h5a RCSB], [http://www.ebi.ac.uk/pdbsum/2h5a 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=2h5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h5a OCA], [http://pdbe.org/2h5a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h5a RCSB], [http://www.ebi.ac.uk/pdbsum/2h5a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h5a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</div>
</div>
<div class="pdbe-citations 2h5a" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2h5a" style="background-color:#fffaf0;"></div>
==See Also==
*[[Phosphomannomutase|Phosphomannomutase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 11:06, 18 October 2017

Complex of the enzyme PMM/PGM with xylose 1-phosphateComplex of the enzyme PMM/PGM with xylose 1-phosphate

Structural highlights

2h5a is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Gene:algC ("Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885)
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

Two complexes of the enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from Pseudomonas aeruginosa with a slow substrate and with an inhibitor have been characterized by X-ray crystallography. Both ligands induce an interdomain rearrangement in the enzyme that creates a highly buried active site. Comparisons with enzyme-substrate complexes show that the inhibitor xylose 1-phosphate utilizes many of the previously observed enzyme-ligand interactions. In contrast, analysis of the ribose 1-phosphate complex reveals a combination of new and conserved enzyme-ligand interactions for binding. The ability of PMM/PGM to accommodate these two pentose phosphosugars in its active site may be relevant for future efforts towards inhibitor design.

Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.,Regni C, Shackelford GS, Beamer LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:16880541[3]

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

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ Regni C, Shackelford GS, Beamer LJ. Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):722-6. Epub 2006 Jul 24. PMID:16880541 doi:10.1107/S1744309106025887

2h5a, resolution 1.72Å

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