3qq5

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^[1]

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