1n8i
From Proteopedia
(Difference between revisions)
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<StructureSection load='1n8i' size='340' side='right'caption='[[1n8i]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1n8i' size='340' side='right'caption='[[1n8i]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1n8i]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1n8i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N8I FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLV:GLYOXYLIC+ACID'>GLV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |
- | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8i OCA], [https://pdbe.org/1n8i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n8i RCSB], [https://www.ebi.ac.uk/pdbsum/1n8i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n8i ProSAT]</span></td></tr> |
- | + | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/MASZ_MYCTU MASZ_MYCTU] Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA (By similarity).[HAMAP-Rule:MF_00641] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n8i ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n8i ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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. | ||
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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:12393860<ref>PMID:12393860</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1n8i" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Malate synthase 3D structures|Malate synthase 3D structures]] | *[[Malate synthase 3D structures|Malate synthase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Malate synthase]] | ||
- | [[Category: Bentrup, K Honer zu]] | ||
- | [[Category: Huang, C C]] | ||
- | [[Category: Miczak, A]] | ||
- | [[Category: Russell, D G]] | ||
- | [[Category: Sacchettini, J C]] | ||
- | [[Category: Smith, C V]] | ||
- | [[Category: Structural genomic]] | ||
- | [[Category: Acetyl coenzyme some]] | ||
- | [[Category: Glcb]] | ||
- | [[Category: Glyoxylate pathway]] | ||
- | [[Category: Isocitrate lyase]] | ||
- | [[Category: Lyase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
- | [[Category: | + | [[Category: Honer zu Bentrup K]] |
- | [[Category: | + | [[Category: Huang CC]] |
- | [[Category: | + | [[Category: Miczak A]] |
+ | [[Category: Russell DG]] | ||
+ | [[Category: Sacchettini JC]] | ||
+ | [[Category: Smith CV]] |
Current revision
Biochemical and Structural Studies of Malate Synthase from Mycobacterium tuberculosis
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