5ubh

Catalytic core domain of Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni with bound ATP

spinqualitylabelsall models 5ubh, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ubh is a 2 chain structure with sequence from Campylobacter jejuni RM1221. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ACT, ATP, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HIS1_CAMJR Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Publication Abstract from PubMed ATP-phosphoribosyltransferase (ATP-PRT) catalyses the first committed step of histidine biosynthesis in plants and micro-organisms. Two forms of ATP-PRT have been reported, which differ in their molecular architecture and mechanism of allosteric regulation. The short-form ATP-PRT is a hetero-octamer, with four HisG chains that comprise only the catalytic domains and four separate chains of HisZ required for allosteric regulation by histidine. The long-form ATP-PRT is homohexameric, with each chain comprising two catalytic domains and a covalently linked regulatory domain that binds histidine as an allosteric inhibitor. Here, we describe a truncated long-form ATP-PRT from Campylobacter jejuni devoid of its regulatory domain ( Cje ATP-PRT(core)). Results showed that Cje ATP-PRT(core) is dimeric, exhibits attenuated catalytic activity, and is insensitive to histidine, indicating the covalently linked regulatory domain plays a role in both catalysis and regulation. Crystal structures were obtained for Cje ATP-PRT(core) in complex with both substrates, and for the first time, the complete product of the reaction. These structures reveal the key features of the active site, and provide insights into how substrates move into position during catalysis. A dimeric catalytic core relates the short and long forms of ATP-phosphoribosyltransferase.,Mittelstadt G, Jiao W, Livingstone E, Moggre GJ, Nazmi AR, Parker EJ Biochem J. 2017 Dec 5. pii: BCJ20170762. doi: 10.1042/BCJ20170762. PMID:29208762 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATP phosphoribosyl transferase 3D structures

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