4q8r: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of a Phosphate Binding Protein (PBP-1) from Clostridium perfringens==
<StructureSection load='4q8r' size='340' side='right' caption='[[4q8r]], [[Resolution|resolution]] 1.65&Aring;' 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.


The entry 4q8r is ON HOLD  until Paper Publication
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>


Authors: Gonzalez, D., Richez, M., Bergonzi, C., Chabriere, E., Elias, M.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of a Phosphate Binding Protein (PBP-1) from Clostridium perfringens
== 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]]
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