Substrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target-Reference-Cited by-同舟云学术

Substrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target

Published:2018-07 Issue:7 Volume:26 Page:948-959.e5
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Atkinson Sarah C.,Dogovski Con,Wood Kathleen,Griffin Michael D.W.,Gorman Michael A.,Hor Lilian,Reboul Cyril F.,Buckle Ashley M.,Wuttke Joachim,Parker Michael W.,Dobson Renwick C.J.,Perugini Matthew A.

Funder

Australian Research Council

Future Fellowships

Australian Cancer Research Foundation

Victorian Government Operational Infrastructure Support Scheme

National Health and Medical Research Council

Commonwealth of Australia

New Zealand Royal Society Marsden Fund

US Army Research Laboratory

US Army Research Office

Biomolecular Interactions Centre

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference105 articles.

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2. Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition;Atkinson;Plant Mol. Biol.,2013

3. Crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine;Atkinson;PLoS One,2012

4. Identification of the bona fide DHDPS from a common plant pathogen;Atkinson;Proteins,2014

5. Crystal structure of dihydrodipicolinate synthase (BA3935) from Bacillus anthracis at 1.94 A resolution;Blagova;Proteins,2006

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