2bvc
|
CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS GLUTAMINE SYNTHETASE IN COMPLEX WITH A TRANSITION STATE MIMIC
OverviewOverview
Glutamine synthetase catalyzes the ligation of glutamate and ammonia to, form glutamine, with the resulting hydrolysis of ATP. The enzyme is a, central component of bacterial nitrogen metabolism and is a potential drug, target. Here, we report a high-yield recombinant expression system for, glutamine synthetase of Mycobacterium tuberculosis together with a simple, purification. The procedure allowed the structure of a complex with a, phosphorylated form of the inhibitor methionine sulfoximine, magnesium, and ADP to be solved by molecular replacement and refined at 2.1-A, resolution. To our knowledge, this study provides the first reported, structure for a taut form of the M. tuberculosis enzyme, similar to that, observed for the Salmonella enzyme earlier. The phospho compound, generated ... [(full description)]
About this StructureAbout this Structure
2BVC is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with MG, CL, P3S and ADP as [ligands]. Active as [Glutamate--ammonia ligase], with EC number [6.3.1.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of Mycobacterium tuberculosis glutamine synthetase in complex with a transition-state mimic provides functional insights., Krajewski WW, Jones TA, Mowbray SL, Proc Natl Acad Sci U S A. 2005 Jul 26;102(30):10499-504. Epub 2005 Jul 18. PMID:16027359
Page seeded by OCA on Tue Oct 30 16:49:05 2007