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3tdx

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Revision as of 18:52, 11 August 2016

Crystal structure of HSC L82V

Structural highlights

3tdx is a 5 chain structure with sequence from Clod6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	3tdo, 3tdp, 3tds, 3tdr, 3te0, 3te1, 3te2
Gene:	CD630_22300, Putative formate/nitrite transporter (CLOD6)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The hydrosulphide ion (HS(-)) and its undissociated form, hydrogen sulphide (H(2)S), which are believed to have been critical to the origin of life on Earth, remain important in physiology and cellular signalling. As a major metabolite in anaerobic bacterial growth, hydrogen sulphide is a product of both assimilatory and dissimilatory sulphate reduction. These pathways can reduce various oxidized sulphur compounds including sulphate, sulphite and thiosulphate. The dissimilatory sulphate reduction pathway uses this molecule as the terminal electron acceptor for anaerobic respiration, in which process it produces excess amounts of H(2)S (ref. 4). The reduction of sulphite is a key intermediate step in all sulphate reduction pathways. In Clostridium and Salmonella, an inducible sulphite reductase is directly linked to the regeneration of NAD(+), which has been suggested to have a role in energy production and growth, as well as in the detoxification of sulphite. Above a certain concentration threshold, both H(2)S and HS(-) inhibit cell growth by binding the metal centres of enzymes and cytochrome oxidase, necessitating a release mechanism for the export of this toxic metabolite from the cell. Here we report the identification of a hydrosulphide ion channel in the pathogen Clostridium difficile through a combination of genetic, biochemical and functional approaches. The HS(-) channel is a member of the formate/nitrite transport family, in which about 50 hydrosulphide ion channels form a third subfamily alongside those for formate (FocA) and for nitrite (NirC). The hydrosulphide ion channel is permeable to formate and nitrite as well as to HS(-) ions. Such polyspecificity can be explained by the conserved ion selectivity filter observed in the channel's crystal structure. The channel has a low open probability and is tightly regulated, to avoid decoupling of the membrane proton gradient.

Identification and characterization of a bacterial hydrosulphide ion channel.,Czyzewski BK, Wang DN Nature. 2012 Mar 11;483(7390):494-7. doi: 10.1038/nature10881. PMID:22407320^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Czyzewski BK, Wang DN. Identification and characterization of a bacterial hydrosulphide ion channel. Nature. 2012 Mar 11;483(7390):494-7. doi: 10.1038/nature10881. PMID:22407320 doi:10.1038/nature10881

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3tdx"

Categories: Clod6 | Czyzewski, B K | Wang, D-N | Membrane protein

@@ Line 1: / Line 1: @@
 ==Crystal structure of HSC L82V==
 <StructureSection load='3tdx' size='340' side='right' caption='[[3tdx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tdo|3tdo]], [[3tdp|3tdp]], [[3tds|3tds]], [[3tdr|3tdr]], [[3te0|3te0]], [[3te1|3te1]], [[3te2|3te2]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CD630_22300, Putative formate/nitrite transporter ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272563 CLOD6])</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=3tdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tdx RCSB], [http://www.ebi.ac.uk/pdbsum/3tdx PDBsum]</span></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=3tdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdx OCA], [http://pdbe.org/3tdx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tdx RCSB], [http://www.ebi.ac.uk/pdbsum/3tdx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tdx ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3tdx" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3tdx

From Proteopedia

Revision as of 18:52, 11 August 2016

Crystal structure of HSC L82V

Structural highlights

Publication Abstract from PubMed

References

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