3klz

<StructureSection load='3klz' size='340' side='right' caption='[[3klz]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[3klz]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KLZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KLZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kly|3kly]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VC_1695 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</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=3klz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3klz OCA], [http://pdbe.org/3klz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3klz RCSB], [http://www.ebi.ac.uk/pdbsum/3klz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3klz ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Formate transport across the inner membrane is a critical step in anaerobic bacterial respiration. Members of the formate/nitrite transport protein family function to shuttle substrate across the cytoplasmic membrane. In bacterial pathogens, the nitrite transport protein is involved in protecting bacteria from peroxynitrite released by host macrophages. We have determined the 2.13-A structure of the formate channel FocA from Vibrio cholerae, which reveals a pentamer in which each monomer possesses its own substrate translocation pore. Unexpectedly, the fold of the FocA monomer resembles that found in water and glycerol channels. The selectivity filter in FocA consists of a cytoplasmic slit and a central constriction ring. A 2.5-A high-formate structure shows two formate ions bound to the cytoplasmic slit via both hydrogen bonding and van der Waals interactions, providing a structural basis for the substrate selectivity of the channel.

Structure and mechanism of a pentameric formate channel.,Waight AB, Love J, Wang DN Nat Struct Mol Biol. 2010 Jan;17(1):31-7. Epub 2009 Dec 13. PMID:20010838<ref>PMID:20010838</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3klz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillo virgola del koch trevisan 1884]]

[[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]]

[[Category: Waight, A B]]

[[Category: Wang, D N]]

[[Category: Structural genomic]]