3git

Crystal structure of a truncated acetyl-CoA synthase

spinqualitylabelsall models 3git, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3git is a 6 chain structure with sequence from Atcc 35608. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, H2S, SF4, SO4, ZN Related: 1oao Gene: acsB2 (ATCC 35608) Activity: Transferase, with EC number 2.3.1.169 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [DCMA_MOOTH] The beta subunit generates CO from CO(2), while the alpha subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the alpha subunit by a corrinoid iron-sulfur protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Ni-dependent acetyl-CoA synthase (ACS) and CO dehydrogenase (CODH) constitute the central enzyme complex of the Wood-Ljungdahl pathway of acetyl-CoA formation. The crystal structure of a recombinant bacterial ACS lacking the N-terminal domain that interacts with CODH shows a large reorganization of the remaining two globular domains, producing a narrow cleft of suitable size, shape, and nature to bind CoA. Sequence comparisons with homologous archaeal enzymes that naturally lack the N-terminal domain show that many amino acids lining this cleft are conserved. Besides the typical [4Fe-4S] center, the A-cluster contains only one proximal metal ion that, according to anomalous scattering data, is most likely Cu or Zn. Incorporation of a functional Ni(2)Fe(4)S(4) A-cluster would require only minor structural rearrangements. Using available structures, a plausible model of the interaction between CODH and the smaller ACS in archaeal multienzyme complexes is presented, along with a discussion of evolutionary relationships of the archaeal and bacterial enzymes. Novel domain arrangement in the crystal structure of a truncated acetyl-CoA synthase from Moorella thermoacetica.,Volbeda A, Darnault C, Tan X, Lindahl PA, Fontecilla-Camps JC Biochemistry. 2009 Aug 25;48(33):7916-26. PMID:19650626 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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