3qq5: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Crystal structure of the [FeFe]-hydrogenase maturation protein HydF== | ||
<StructureSection load='3qq5' size='340' side='right' caption='[[3qq5]], [[Resolution|resolution]] 2.99Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3qq5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_neapolitana Thermotoga neapolitana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QQ5 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1feh|1feh]], [[3ciw|3ciw]], [[3lx4|3lx4]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTN_0227 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2337 Thermotoga neapolitana])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qq5 RCSB], [http://www.ebi.ac.uk/pdbsum/3qq5 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
[FeFe]-hydrogenases catalyze the reversible pro-duction of H2 in some bacteria and unicellular eu-karyotes. These enzymes require ancillary proteins to assemble the unique active site H-cluster, a com-plex structure composed of a 2Fe center bridged to a [4Fe-4S] cubane. The first crystal structure of a key factor in the maturation process, HydF, has been determined at 3A resolution. The protein monomer present in the asymmetric unit of the crystal comprises three domains: a GTP-binding domain, a dimerization domain and a metal-cluster binding domain, all characterized by similar fold-ing motifs. Two monomers dimerize, giving rise to a stable dimer, held together mainly by the for-mation of a continuous beta-sheet comprising eight beta-strands from two monomers. Moreover, in the structure presented two dimers aggregate to form a supramolecular organization that represents an in-activated form of the HydF maturase. The crystal structure of the latter furnishes several clues about the events necessary for cluster genera-tion/transfer, and provides an excellent model to begin elucidating the structure/function of HydF in [FeFe]-hydrogenase maturation. | |||
Crystal structure of HydF scaffold protein provides insights into [FeFe]-hydrogenase maturation.,Cendron L, Berto P, D'Adamo S, Vallese F, Govoni C, Posewitz MC, Giacometti GM, Costantini P, Zanotti G J Biol Chem. 2011 Nov 4. PMID:22057316<ref>PMID:22057316</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[GTP-binding protein|GTP-binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Thermotoga neapolitana]] | [[Category: Thermotoga neapolitana]] | ||
[[Category: Adamo, S D.]] | [[Category: Adamo, S D.]] | ||
Revision as of 05:24, 4 June 2014
Crystal structure of the [FeFe]-hydrogenase maturation protein HydF
| ||||||||||||
