1n8i: Difference between revisions
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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> | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8i OCA], [http://www.ebi.ac.uk/pdbsum/1n8i PDBsum | |RELATEDENTRY=[[1n8w|1N8W]] | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8i OCA], [http://www.ebi.ac.uk/pdbsum/1n8i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n8i RCSB]</span> | |||
}} | }} | ||
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[[Category: tbsgc]] | [[Category: tbsgc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:26:52 2008'' | ||
Revision as of 19:26, 30 March 2008
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| 1n8i, resolution 2.1Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | GLV, MG | ||||||||||||
| Gene: | GLCB (Mycobacterium tuberculosis) | ||||||||||||
| Activity: | Malate synthase, with EC number 2.3.3.9 | ||||||||||||
| Domains: | malate_synt_G | ||||||||||||
| Related: | 1N8W
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| 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
1N8I 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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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Malate synthase
- Mycobacterium tuberculosis
- Single protein
- Bentrup, K Honer zu.
- Huang, C C.
- Miczak, A.
- Russell, D G.
- Sacchettini, J C.
- Smith, C V.
- TBSGC, TB Structural Genomics Consortium.
- Acetyl coenzyme some
- Glcb
- Glyoxylate pathway
- Isocitrate lyase
- Persistence
- Protein structure initiative
- Psi
- Structural genomic
- Tb structural genomics consortium
- Tbsgc
