Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/79246
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Type: Journal article
Title: Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: An antibiotic target
Author: Pendini, N.
Yap, M.
Polyak, S.
Cowieson, N.
Abell, A.
Booker, G.
Wallace, J.
Wilce, J.
Wilce, M.
Citation: Protein Science, 2013; 22(6):762-773
Publisher: Cold Spring Harbor Lab Press
Issue Date: 2013
ISSN: 0961-8368
1469-896X
Statement of
Responsibility: 
Nicole R. Pendini, Min Y. Yap, Steven W. Polyak, Nathan P. Cowieson, Andrew Abell, Grant W. Booker, John C. Wallace, Jacqueline A. Wilce, and Matthew C. J. Wilce
Abstract: The essential metabolic enzyme biotin protein ligase (BPL) is a potential target for the development of new antibiotics required to combat drug-resistant pathogens. Staphylococcus aureus BPL (SaBPL) is a bifunctional protein, possessing both biotin ligase and transcription repressor activities. This positions BPL as a key regulator of several important metabolic pathways. Here, we report the structural analysis of both holo- and apo-forms of SaBPL using X-ray crystallography. We also present small-angle X-ray scattering data of SaBPL in complex with its biotin-carboxyl carrier protein substrate as well as the SaBPL:DNA complex that underlies repression. This has revealed the molecular basis of ligand (biotinyl-5'-AMP) binding and conformational changes associated with catalysis and repressor function. These data provide new information to better understand the bifunctional activities of SaBPL and to inform future strategies for antibiotic discovery.
Keywords: biotin protein ligase; biotin-carboxyl carrier protein; DNA-binding; bacterial enzyme; biotinylation; small-angle X-ray scattering
Description: Corrected by: Erratum: Structural characterisation of Staphylococcus aureus biotin protein ligase and interaction partners: An antibiotic target, in Vol. 23, Issue 1, 121. Daouda Traore, was inadvertently omitted from the published version of their manuscript.
Rights: © 2013 The Protein Society
RMID: 0020130273
DOI: 10.1002/pro.2262
Appears in Collections:Molecular and Biomedical Science publications

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