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[[Image:1pcj.jpg|left|200px]]
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{{STRUCTURE_1pcj|  PDB=1pcj  |  SCENE=  }}
'''Enzyme-ligand complex of P. aeruginosa PMM/PGM'''


==Enzyme-ligand complex of P. aeruginosa PMM/PGM==
<StructureSection load='1pcj' size='340' side='right'caption='[[1pcj]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pcj]] 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=1PCJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PCJ FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M1P:ALPHA-D-MANNOSE+1-PHOSPHATE'>M1P</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1pcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcj OCA], [https://pdbe.org/1pcj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pcj RCSB], [https://www.ebi.ac.uk/pdbsum/1pcj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pcj ProSAT]</span></td></tr>
</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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/1pcj_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=1pcj ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzyme-substrate complexes of phosphomannomutase/phosphoglucomutase (PMM/PGM) reveal the structural basis of the enzyme's ability to use four different substrates in catalysis. High-resolution structures with glucose 1-phosphate, glucose 6-phosphate, mannose 1-phosphate, and mannose 6-phosphate show that the position of the phosphate group of each substrate is held constant by a conserved network of hydrogen bonds. This produces two distinct, and mutually exclusive, binding orientations for the sugar rings of the 1-phospho and 6-phospho sugars. Specific binding of both orientations is accomplished by key contacts with the O3 and O4 hydroxyls of the sugar, which must occupy equatorial positions. Dual recognition of glucose and mannose phosphosugars uses a combination of specific protein contacts and nonspecific solvent contacts. The ability of PMM/PGM to accommodate these four diverse substrates in a single active site is consistent with its highly reversible phosphoryl transfer reaction and allows it to function in multiple biosynthetic pathways in P. aeruginosa.


==Overview==
Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.,Regni C, Naught L, Tipton PA, Beamer LJ Structure. 2004 Jan;12(1):55-63. PMID:14725765<ref>PMID:14725765</ref>
Enzyme-substrate complexes of phosphomannomutase/phosphoglucomutase (PMM/PGM) reveal the structural basis of the enzyme's ability to use four different substrates in catalysis. High-resolution structures with glucose 1-phosphate, glucose 6-phosphate, mannose 1-phosphate, and mannose 6-phosphate show that the position of the phosphate group of each substrate is held constant by a conserved network of hydrogen bonds. This produces two distinct, and mutually exclusive, binding orientations for the sugar rings of the 1-phospho and 6-phospho sugars. Specific binding of both orientations is accomplished by key contacts with the O3 and O4 hydroxyls of the sugar, which must occupy equatorial positions. Dual recognition of glucose and mannose phosphosugars uses a combination of specific protein contacts and nonspecific solvent contacts. The ability of PMM/PGM to accommodate these four diverse substrates in a single active site is consistent with its highly reversible phosphoryl transfer reaction and allows it to function in multiple biosynthetic pathways in P. aeruginosa.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1PCJ is a [[Single protein]] 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=1PCJ OCA].
</div>
<div class="pdbe-citations 1pcj" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa., Regni C, Naught L, Tipton PA, Beamer LJ, Structure. 2004 Jan;12(1):55-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14725765 14725765]
*[[Phosphomannomutase|Phosphomannomutase]]
[[Category: Phosphomannomutase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Beamer LJ]]
[[Category: Beamer, L J.]]
[[Category: Regni C]]
[[Category: Regni, C.]]
[[Category: Tipton PA]]
[[Category: Tipton, P A.]]
[[Category: Alpha/beta protein]]
[[Category: Enzyme-ligand complex]]
[[Category: Enzyme-metal complex]]
[[Category: Phosphohexomutase]]
[[Category: Phosphoserine]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:56:18 2008''
Retrieved from "https://proteopedia.org/1pcj"