1n8w

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[[Image:1n8w.gif|left|200px]]<br /><applet load="1n8w" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n8w.gif|left|200px]]
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caption="1n8w, resolution 2.70&Aring;" />
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'''Biochemical and Structural Studies of Malate Synthase from Mycobacterium tuberculosis'''<br />
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{{Structure
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|PDB= 1n8w |SIZE=350|CAPTION= <scene name='initialview01'>1n8w</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MLT:MALATE+ION'>MLT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene> and <scene name='pdbligand=GLV:GLYOXYLIC ACID'>GLV</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.9 2.3.3.9]
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|GENE= GlcB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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}}
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'''Biochemical and Structural Studies of Malate Synthase from Mycobacterium tuberculosis'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1N8W 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=SO4:'>SO4</scene>, <scene name='pdbligand=MLT:'>MLT</scene>, <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=GLV:'>GLV</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Malate_synthase Malate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.9 2.3.3.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8W OCA].
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1N8W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8W OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12393860 12393860]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12393860 12393860]
[[Category: Malate synthase]]
[[Category: Malate synthase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: MLT]]
[[Category: MLT]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: coenzyme a]]
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[[Category: coenzyme some]]
[[Category: glcb]]
[[Category: glcb]]
[[Category: glyoxylate]]
[[Category: glyoxylate]]
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[[Category: protein structure initiative]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: tb structural genomics consortium]]
[[Category: tb structural genomics consortium]]
[[Category: tbsgc]]
[[Category: tbsgc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:53:40 2008''

Revision as of 10:53, 20 March 2008


PDB ID 1n8w

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