6jv1

Crystal Structure of N-terminal domain of ArgZ, C264S mutant, bound to Substrate, an arginine dihydrolase from the Ornithine-Ammonia Cycle in Cyanobacteria

spinqualitylabelsall models 6jv1, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jv1 is a 1 chain structure with sequence from Synechocystis sp. PCC 6803 substr. Kazusa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.2Å Ligands: ARG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P74535_SYNY3 Publication Abstract from PubMed A recently discovered ornithine-ammonia cycle (OAC) serves as a conduit in the nitrogen storage-and-remobilization machinery in cyanobacteria. The OAC involves an arginine-catabolic reaction catalyzed by the arginine dihydrolase ArgZ whose catalytic mechanism is unknown. Here, we determined the crystal structures at 1.2-3.0 A of unliganded ArgZ from the cyanobacterium Synechocystis sp. PCC6803 and of ArgZ complexed with its substrate arginine, a covalently linked reaction intermediate, or the reaction product ornithine. The structures reveal that a key residue, Asn(71), in the ArgZ active center, functions as the determinant distinguishing ArgZ from other members of the guanidino group-modifying enzyme superfamily. The structures, along with biochemical evidence from enzymatic assays coupled with electrospray ionization MS (ESI-MS) techniques, further suggest that ArgZ-catalyzed conversion of arginine to ornithine, ammonia, and carbon dioxide by ArgZ consists of two successive cycles of amine hydrolysis. Finally, we show that arginine dihydrolases are broadly distributed among bacteria and metazoan, suggesting that the OAC may be frequently used for redistribution of nitrogen from arginine catabolism or nitrogen fixation. Crystal structures and biochemical analyses of the bacterial arginine dihydrolase ArgZ suggests a "bond-rotation" catalytic mechanism.,Zhuang N, Zhang H, Li L, Wu X, Yang C, Zhang Y J Biol Chem. 2019 Dec 30. pii: RA119.011752. doi: 10.1074/jbc.RA119.011752. PMID:31914412 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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