2h4l
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2h4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h4l, resolution 2.40Å" /> '''Complex of PMM/PGM w...) |
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| - | [[Image:2h4l.gif|left|200px]]<br /><applet load="2h4l" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2h4l, resolution 2.40Å" /> | ||
| - | '''Complex of PMM/PGM with ribose 1-phosphate'''<br /> | ||
| - | == | + | ==Complex of PMM/PGM with ribose 1-phosphate== |
| - | Two complexes of the enzyme phosphomannomutase/phosphoglucomutase | + | <StructureSection load='2h4l' size='340' side='right'caption='[[2h4l]], [[Resolution|resolution]] 2.40Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2h4l]] 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=2H4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H4L 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]] 2.4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=R1P:RIBOSE-1-PHOSPHATE'>R1P</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=2h4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4l OCA], [https://pdbe.org/2h4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h4l RCSB], [https://www.ebi.ac.uk/pdbsum/2h4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h4l 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/h4/2h4l_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=2h4l ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:16880541</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2h4l" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Phosphomannomutase|Phosphomannomutase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa]] | ||
| + | [[Category: Beamer LJ]] | ||
Current revision
Complex of PMM/PGM with ribose 1-phosphate
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