View source for 2auv


==Solution Structure of HndAc : A Thioredoxin-like [2Fe-2S] Ferredoxin Involved in the NADP-reducing Hydrogenase Complex==
<StructureSection load='2auv' size='340' side='right'caption='[[2auv]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2auv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Solidesulfovibrio_fructosivorans Solidesulfovibrio fructosivorans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AUV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR,  models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=2auv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2auv OCA], [https://pdbe.org/2auv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2auv RCSB], [https://www.ebi.ac.uk/pdbsum/2auv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2auv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HNDA_SOLFR HNDA_SOLFR] Catalyzes the reduction of NADP in the presence of molecular H(2) to yield NADPH.<ref>PMID:7751270</ref> <ref>PMID:9703971</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/2auv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2auv ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The NADP-reducing hydrogenase complex from Desulfovibrio fructosovorans is a heterotetramer encoded by the hndABCD operon. Sequence analysis indicates that the HndC subunit (52 kDa) corresponds to the NADP-reducing unit, and the HndD subunit (63.5 kDa) is homologous to Clostridium pasteurianum hydrogenase. The role of HndA and HndB subunits (18.8 kDa and 13.8 kDa, respectively) in the complex remains unknown. The HndA subunit belongs to the [2Fe-2S] ferredoxin family typified by C. pasteurianum ferredoxin. HndA is organized into two independent structural domains, and we report in the present work the NMR structure of its C-terminal domain, HndAc. HndAc has a thioredoxin-like fold consisting in four beta-strands and two relatively long helices. The [2Fe-2S] cluster is located near the surface of the protein and bound to four cysteine residues particularly well conserved in this class of proteins. Electron exchange between the HndD N-terminal [2Fe-2S] domain (HndDN) and HndAc has been previously evidenced, and in the present studies we have mapped the binding site of the HndDN domain on HndAc. A structural analysis of HndB indicates that it is a FeS subunit with 41% similarity with HndAc and it contains a possible thioredoxin-like fold. Our data let us propose that HndAc and HndB can form a heterodimeric intermediate in the electron transfer between the hydrogenase (HndD) active site and the NADP reduction site in HndC.

Solution structure of HndAc: a thioredoxin-like domain involved in the NADP-reducing hydrogenase complex.,Nouailler M, Morelli X, Bornet O, Chetrit B, Dermoun Z, Guerlesquin F Protein Sci. 2006 Jun;15(6):1369-78. PMID:16731971<ref>PMID:16731971</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 2auv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Solidesulfovibrio fructosivorans]]
[[Category: Bornet O]]
[[Category: Chetrit B]]
[[Category: Dermoun Z]]
[[Category: Guerlesquin F]]
[[Category: Morelli X]]
[[Category: Nouailler M]]