University of Sussex
Browse

File(s) not publicly available

The crystal structure of UMP Kinase from Bacillus anthracis (BA1797) reveals an allosteric nucleotide-binding site

journal contribution
posted on 2023-06-08, 19:50 authored by Christoph Meier, Lester G Carter, Sarah Sainsbury, Erika ManciniErika Mancini, Raymond J Owens, David I Stuart, Robert M Esnouf
Uridine monophosphate (UMP) kinase is a conserved enzyme that catalyzes the ATP-driven conversion of uridylate monophosphate into uridylate diphosphate, an essential metabolic step. In prokaryotes, the enzyme exists as a homohexamer that is regulated by various metabolites. Whereas the enzymatic mechanism of UMP kinase (UK) is well-characterized, the molecular basis of its regulation remains poorly understood. Here we report the crystal structure of UK from Bacillus anthracis (BA1797) in complex with ATP at 2.82 Å resolution. It reveals that the cofactor, in addition to binding in the active sites, also interacts with separate binding pockets located near the center of the hexameric structure. The existence of such an allosteric binding site had been predicted by biochemical studies, but it was not identified in previous crystal structures of prokaryotic UKs. We show that this putative allosteric pocket is conserved across different bacterial species, suggesting that it is a feature common to bacterial UKs, and we present a structural model for the allosteric regulation of this enzyme. © 2008 Elsevier Ltd. All rights reserved.

History

Publication status

  • Published

Journal

Journal of Molecular Biology

ISSN

0022-2836

Publisher

Elsevier

Issue

5

Volume

381

Page range

1098-1105

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2015-01-30

Usage metrics

    University of Sussex (Publications)

    Categories

    No categories selected

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC