1n8w

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|GENE= GlcB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
|GENE= GlcB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00728 malate_synt_G]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00728 malate_synt_G]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8w OCA], [http://www.ebi.ac.uk/pdbsum/1n8w PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1n8w RCSB]</span>
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|RELATEDENTRY=[[1n8i|1N8I]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8w OCA], [http://www.ebi.ac.uk/pdbsum/1n8w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n8w RCSB]</span>
}}
}}
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[[Category: tbsgc]]
[[Category: tbsgc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:57:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:26:58 2008''

Revision as of 19:26, 30 March 2008

Image:1n8w.gif


PDB ID 1n8w

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands: , , , ,
Gene: GlcB (Mycobacterium tuberculosis)
Activity: Malate synthase, with EC number 2.3.3.9
Domains: malate_synt_G
Related: 1N8I


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Biochemical and Structural Studies of Malate Synthase from Mycobacterium tuberculosis


Overview

Establishment or maintenance of a persistent infection by Mycobacterium tuberculosis requires the glyoxylate pathway. This is a bypass of the tricarboxylic acid cycle in which isocitrate lyase and malate synthase (GlcB) catalyze the net incorporation of carbon during growth of microorganisms on acetate or fatty acids as the primary carbon source. The glcB gene from M. tuberculosis, which encodes malate synthase, was cloned, and GlcB was expressed in Escherichia coli. The influence of media conditions on expression in M. tuberculosis indicated that this enzyme is regulated differentially to isocitrate lyase. Purified GlcB had K(m) values of 57 and 30 microm for its substrates glyoxylate and acetyl coenzyme A, respectively, and was inhibited by bromopyruvate, oxalate, and phosphoenolpyruvate. The GlcB structure was solved to 2.1-A resolution in the presence of glyoxylate and magnesium. We also report the structure of GlcB in complex with the products of the reaction, coenzyme A and malate, solved to 2.7-A resolution. Coenzyme A binds in a bent conformation, and the details of its interactions are described, together with implications on the enzyme mechanism.

About this Structure

1N8W is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Biochemical and structural studies of malate synthase from Mycobacterium tuberculosis., Smith CV, Huang CC, Miczak A, Russell DG, Sacchettini JC, Honer zu Bentrup K, J Biol Chem. 2003 Jan 17;278(3):1735-43. Epub 2002 Oct 21. PMID:12393860

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