2bvc: Difference between revisions
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[[Image:2bvc.gif|left|200px]]<br /><applet load="2bvc" size=" | [[Image:2bvc.gif|left|200px]]<br /><applet load="2bvc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2bvc, resolution 2.10Å" /> | caption="2bvc, resolution 2.10Å" /> | ||
'''CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS GLUTAMINE SYNTHETASE IN COMPLEX WITH A TRANSITION STATE MIMIC'''<br /> | '''CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS GLUTAMINE SYNTHETASE IN COMPLEX WITH A TRANSITION STATE MIMIC'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2BVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with MG, CL, P3S and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain F'>AC1</scene>. Full crystallographic information is available from [http:// | 2BVC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=P3S:'>P3S</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+F'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BVC OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transition state mimic]] | [[Category: transition state mimic]] | ||
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Revision as of 11:28, 3 February 2008
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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 in situ by an active enzyme, mimics the phosphorylated, tetrahedral adduct at the transition state. Some differences in ligand, interactions of the protein with both phosphorylated compound and, nucleotide are observed compared with earlier structures; a third metal, ion also is found. The importance of these differences in the catalytic, mechanism is discussed; the results will help guide the search for, specific inhibitors of potential therapeutic interest.
About this StructureAbout this Structure
2BVC is a Single protein structure of sequence from Mycobacterium tuberculosis with , , and as ligands. Active as Glutamate--ammonia ligase, with EC number 6.3.1.2 Known structural/functional Site: . 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
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