8aio: Difference between revisions

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'''Unreleased structure'''


The entry 8aio is ON HOLD  until Paper Publication
==CO-bound [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI)==
<StructureSection load='8aio' size='340' side='right'caption='[[8aio]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8aio]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AIO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MHX:1,1,7-tris(hydroxymethyl)-8-oxidanylidene-2$l^{3},6$l^{3}-dithia-4-aza-1$l^{6},7$l^{5}-diferratricyclo[4.2.0.0^{2,7}]octane-1,7-dicarbonitrile'>MHX</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=8aio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aio OCA], [https://pdbe.org/8aio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aio RCSB], [https://www.ebi.ac.uk/pdbsum/8aio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aio ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHF1_CLOPA PHF1_CLOPA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hydrogenases are H2 converting enzymes that harbor catalytic cofactors in which iron (Fe) ions are coordinated by biologically unusual carbon monoxide (CO) and cyanide (CN-) ligands. Extrinsic CO and CN-, however, inhibit hydrogenases. The mechanism by which CN- binds to [FeFe]-hydrogenases is not known. Here, we obtained crystal structures of the CN--treated [FeFe]-hydrogenase CpI from Clostridium pasteurianum. The high resolution of 1.39 A allowed us to distinguish intrinsic CN- and CO ligands and to show that extrinsic CN- binds to the open coordination site of the cofactor where CO is known to bind. In contrast to other inhibitors, CN- treated crystals show conformational changes of conserved residues within the proton transfer pathway which could allow a direct proton transfer between E279 and S319. This configuration has been proposed to be vital for efficient proton transfer, but has never been observed structurally.


Authors:  
Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.,Duan J, Hemschemeier A, Burr DJ, Stripp ST, Hofmann E, Happe T Angew Chem Int Ed Engl. 2022 Dec 4. doi: 10.1002/anie.202216903. PMID:36464641<ref>PMID:36464641</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8aio" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium pasteurianum]]
[[Category: Large Structures]]
[[Category: Duan J]]
[[Category: Happe T]]
[[Category: Hofmann E]]
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