4yb5

Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with the allosteric inhibitor histidine

spinqualitylabelsall models 4yb5, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yb5 is a 6 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 2.24Å Ligands: HIS, K, PEG, PGE, SCN 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 Adenosine triphosphate phosphoribosyltransferase (ATP-PRT) catalyzes the first committed step of the histidine biosynthesis in plants and microorganisms. Here, we present the functional and structural characterization of the ATP-PRT from the pathogenic epsilon-proteobacteria Campylobacter jejuni (CjeATP-PRT). This enzyme is a member of the long form (HisGL ) ATP-PRT and is allosterically inhibited by histidine, which binds to a remote regulatory domain, and competitively inhibited by AMP. In the crystalline form, CjeATP-PRT was found to adopt two distinctly different hexameric conformations, with an open homohexameric structure observed in the presence of substrate ATP, and a more compact closed form present when inhibitor histidine is bound. CjeATP-PRT was observed to adopt only a hexameric quaternary structure in solution, contradicting previous hypotheses favoring an allosteric mechanism driven by an oligomer equilibrium. Instead, this study supports the conclusion that the ATP-PRT long form hexamer is the active species; the tightening of this structure in response to remote histidine binding results in an inhibited enzyme. Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer that is allosterically controlled by the twisting of a regulatory tail.,Mittelstadt G, Moggre GJ, Panjikar S, Nazmi AR, Parker EJ Protein Sci. 2016 Aug;25(8):1492-506. doi: 10.1002/pro.2948. Epub 2016 Jun 6. PMID:27191057 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATP phosphoribosyl transferase 3D structures

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