2ycl

complete structure of the corrinoid,iron-sulfur protein including the N-terminal domain with a 4Fe-4S cluster

spinqualitylabelsall models 2ycl, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ycl is a 2 chain structure with sequence from Carboxydothermus hydrogenoformans z-2901. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: B12, SF4 Related: 2yck, 2yci, 2ycj Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Several anaerobic acetogenic, methanogenic, hydrogenogenic, and sulfate-reducing microorganisms are able to use the reductive acetyl-CoA (Wood-Ljungdahl) pathway to convert CO(2) into biomass. The reductive acetyl-CoA pathway consists of two branches connected by the Co/Fe-containing corrinoid iron-sulfur protein (CoFeSP), which transfers a methyl group from a methyltransferase (MeTr)/methyltetrahydrofolate (CH(3)-H(4) folate) complex to the reduced Ni-Ni-[4Fe-4S] cluster (cluster A) of acetyl-CoA synthase. We investigated the CoFeSP and MeTr couple of the hydrogenogenic bacterium Carboxydothermus hydrogenoformans and show that the two proteins are able to catalyze the methyl-group transfer reaction from CH(3)-H(4) folate to the Co(I) center of CoFeSP. We determined the crystal structures of both proteins. The structure of CoFeSP includes the previously unresolved N-terminal domain of the large subunit of CoFeSP, revealing a unique four-helix-bundle-like architecture in which a [4Fe-4S] cluster is shielded by hydrophobic amino acids. It further reveals that the corrinoid and the [4Fe-4S] cluster binding domains are mobile, which is mandatory for the postulated electron transfer between them. Furthermore, we solved the crystal structures of apo-MeTr, CH(3)-H(4)-folate-bound MeTr, and H(4)-folate-bound MeTr, revealing a substrate-induced closure of the CH(3)-H(4) folate binding cavity of MeTr. We observed three different conformations of Asn200 depending on the substrate bound in the active site, demonstrating its conformational modulation by hydrogen-bonding interactions with the substrate. The observed flexibility could be essential to stabilize the transition state during methyl-group transfer. The conformational space and role of Asn200 are likely conserved in homologous cobalamin-dependent MeTrs such as methionine synthase. Structural Basis for Electron and Methyl-Group Transfer in a Methyltransferase System Operating in the Reductive Acetyl-CoA Pathway.,Goetzl S, Jeoung JH, Hennig SE, Dobbek H J Mol Biol. 2011 Aug 5;411(1):96-109. Epub 2011 May 27. PMID:21640123 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acetyl-CoA synthase Carbon monoxide dehydrogenase

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