4q8r
From Proteopedia
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| - | ''' | + | ==Crystal structure of a Phosphate Binding Protein (PBP-1) from Clostridium perfringens== |
| + | <StructureSection load='4q8r' size='340' side='right' caption='[[4q8r]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4q8r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q8R FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gd5|4gd5]]</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=4q8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q8r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q8r RCSB], [http://www.ebi.ac.uk/pdbsum/4q8r PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phosphate limitation is an important environmental stress that affects the metabolism of various organisms and, in particular, can trigger the virulence of numerous bacterial pathogens. Clostridium perfringens, a human pathogen, is one of the most common causes of enteritis necroticans, gas gangrene and food poisoning. Here, we focused on the high affinity phosphate-binding protein (PBP-1) of an ABC-type transporter, responsible for cellular phosphate uptake. We report the crystal structure (1.65 A resolution) of the protein in complex with phosphate. Interestingly, PBP-1 does not form the short, low-barrier hydrogen bond with phosphate that is typical of previously characterized phosphate-binding proteins, but rather a canonical hydrogen bond. In its unique binding configuration, PBP-1 forms an unusually high number of hydrogen bonds (14) with the phosphate anion. Discrimination experiments reveal that PBP-1 is the least selective PBP characterised so far and is able to discriminate phosphate from its close competing anion, arsenate, by ~150-fold. | ||
| - | + | Crystal structure of the phosphate-binding protein (PBP-1) of an ABC-type phosphate transporter from Clostridium perfringens.,Gonzalez D, Richez M, Bergonzi C, Chabriere E, Elias M Sci Rep. 2014 Oct 16;4:6636. doi: 10.1038/srep06636. PMID:25338617<ref>PMID:25338617</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bergonzi, C.]] | ||
| + | [[Category: Chabriere, E.]] | ||
| + | [[Category: Elias, M.]] | ||
| + | [[Category: Gonzalez, D.]] | ||
| + | [[Category: Richez, M.]] | ||
| + | [[Category: Periplasmic high affinity phosphate binding protein]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 08:44, 5 November 2014
Crystal structure of a Phosphate Binding Protein (PBP-1) from Clostridium perfringens
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