5lad: Difference between revisions

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New page: '''Unreleased structure''' The entry 5lad is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 5lad is ON HOLD  until Paper Publication
==Crystal Structure of apo HydF from thermotoga maritima==
<StructureSection load='5lad' size='340' side='right'caption='[[5lad]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lad]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LAD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=5lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lad OCA], [https://pdbe.org/5lad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lad RCSB], [https://www.ebi.ac.uk/pdbsum/5lad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lad ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9WYS6_THEMA Q9WYS6_THEMA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
[FeFe] hydrogenase (HydA) catalyzes interconversion between 2H+ and H2 at an active site composed of a [4Fe-4S] cluster linked to a 2Fe subcluster that harbors CO, CN- and azapropanedithiolate (adt2-) ligands. HydE, HydG and HydF are the maturases specifically involved in the biosynthesis of the 2Fe subcluster. Using ligands synthesized by HydE and HydG, HydF assembles a di-iron precursor of the 2Fe subcluster and transfers it to HydA for maturation. Here we report the first X-ray structure of HydF with its [4Fe-4S] cluster. The cluster is chelated by three cysteines and an exchangeable glutamate, which allows the binding of synthetic mimics of the 2Fe subcluster. [Fe2(adt)(CO)4(CN)2]2- is proposed to be the true di-iron precursor because, when bound to HydF, it matures HydA and displays features in Fourier transform infrared (FTIR) spectra that are similar to those of the native HydF active intermediate. A new route toward the generation of artificial hydrogenases, as combinations of HydF and such biomimetic complexes, is proposed on the basis of the observed hydrogenase activity of chemically modified HydF.


Authors:  
Structural and functional characterization of the hydrogenase-maturation HydF protein.,Caserta G, Pecqueur L, Adamska-Venkatesh A, Papini C, Roy S, Artero V, Atta M, Reijerse E, Lubitz W, Fontecave M Nat Chem Biol. 2017 Jul;13(7):779-784. doi: 10.1038/nchembio.2385. Epub 2017 May , 29. PMID:28553946<ref>PMID:28553946</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 5lad" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Caserta G]]
[[Category: Fontecave M]]
[[Category: Pecqueur L]]
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