4YB7

Adenosine triphosphate phosphoribosyltransferase from Campylobacter jejuni in complex with ATP

Summary for 4YB7

• Entry DOI: 10.2210/pdb4yb7/pdb
• Related: 4YB5 4YB6
• Descriptor: ATP phosphoribosyltransferase, MAGNESIUM ION, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: phosphoribosyltransferase, hexamer, atp, transferase
• Biological source: Campylobacter jejuni (strain RM1221)
• Total number of polymer chains: 12
• Total formula weight: 411902.76

Authors

Mittelstaedt, G.,Moggre, G.-J.,Parker, E.J. (deposition date: 2015-02-18, release date: 2016-03-09, Last modification date: 2024-10-23)

Primary citation

Mittelstadt, G.,Moggre, G.J.,Panjikar, S.,Nazmi, A.R.,Parker, E.J.
Campylobacter jejuni adenosine triphosphate phosphoribosyltransferase is an active hexamer that is allosterically controlled by the twisting of a regulatory tail.
Protein Sci., 25:1492-1506, 2016

PubMed Abstract: 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 ε-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.

PubMed: 27191057
DOI: 10.1002/pro.2948

Experimental method

X-RAY DIFFRACTION (2.2 Å)