4rtb | pdb_00004rtb

X-ray structure of the FeFe-hydrogenase maturase HydG from Carboxydothermus hydrogenoformans

spinqualitylabelsall models 4rtb, resolution 2.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rtb is a 1 chain structure with sequence from Carhz. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, SAM, SF4 Gene: CHY_1549 (CARHZ) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The structure of the radical S-adenosyl-L-methionine (SAM) [FeFe]-hydrogenase maturase HydG involved in CN- /CO synthesis is characterized by two internal tunnels connecting its tyrosine-binding pocket with the external medium and the C-terminal Fe4 S4 cluster-containing region. A comparison with a tryptophan-bound NosL structure suggests that substrate binding causes the closing of the first tunnel and, along with mutagenesis studies, that tyrosine binds to HydG with its amino group well positioned for H-abstraction by SAM. In this orientation the dehydroglycine (DHG) fragment caused by tyrosine CalphaCbeta bond scission can readily migrate through the second tunnel towards the C-terminal domain where both CN- and CO are synthesized. Our HydG structure appears to be in a relaxed state with its C-terminal cluster CysX2 CysX22 Cys motif exposed to solvent. A rotation of this domain coupled to Fe4 S4 cluster assembly would bury its putatively reactive unique Fe ion thereby allowing it to interact with DHG. Crystal Structure of HydG from Carboxydothermus hydrogenoformans: A Trifunctional [FeFe]-Hydrogenase Maturase.,Nicolet Y, Pagnier A, Zeppieri L, Martin L, Amara P, Fontecilla-Camps JC Chembiochem. 2014 Dec 10. doi: 10.1002/cbic.201402661. PMID:25504963 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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