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1w66
From Proteopedia
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|PDB= 1w66 |SIZE=350|CAPTION= <scene name='initialview01'>1w66</scene>, resolution 1.08Å | |PDB= 1w66 |SIZE=350|CAPTION= <scene name='initialview01'>1w66</scene>, resolution 1.08Å | ||
|SITE= <scene name='pdbsite=AC1:Dka+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Dka+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=DKA:DECANOIC ACID'>DKA</scene> | + | |LIGAND= <scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w66 OCA], [http://www.ebi.ac.uk/pdbsum/1w66 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w66 RCSB]</span> | ||
}} | }} | ||
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[[Category: Wilmanns, M.]] | [[Category: Wilmanns, M.]] | ||
[[Category: XMTB, Mycobacterium Tuberculosis Structural Proteomics Project.]] | [[Category: XMTB, Mycobacterium Tuberculosis Structural Proteomics Project.]] | ||
| - | [[Category: DKA]] | ||
[[Category: acyltransferase]] | [[Category: acyltransferase]] | ||
[[Category: lipoate-protein ligase b]] | [[Category: lipoate-protein ligase b]] | ||
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[[Category: xmtb]] | [[Category: xmtb]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:31:47 2008'' |
Revision as of 21:31, 30 March 2008
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| , resolution 1.08Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A LIPOATE-PROTEIN LIGASE B FROM MYCOBACTERIUM TUBERCULOSIS
Overview
Lipoic acid is essential for the activation of a number of protein complexes involved in key metabolic processes. Growth of Mycobacterium tuberculosis relies on a pathway in which the lipoate attachment group is synthesized from an endogenously produced octanoic acid moiety. In patients with multiple-drug-resistant M. tuberculosis, expression of one gene from this pathway, lipB, encoding for octanoyl-[acyl carrier protein]-protein acyltransferase is considerably up-regulated, thus making it a potential target in the search for novel antiinfectives against tuberculosis. Here we present the crystal structure of the M. tuberculosis LipB protein at atomic resolution, showing an unexpected thioether-linked active-site complex with decanoic acid. We provide evidence that the transferase functions as a cysteine/lysine dyad acyltransferase, in which two invariant residues (Lys-142 and Cys-176) are likely to function as acid/base catalysts. Analysis by MS reveals that the LipB catalytic reaction proceeds by means of an internal thioesteracyl intermediate. Structural comparison of LipB with lipoate protein ligase A indicates that, despite conserved structural and sequence active-site features in the two enzymes, 4'-phosphopantetheine-bound octanoic acid recognition is a specific property of LipB.
About this Structure
1W66 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase., Ma Q, Zhao X, Nasser Eddine A, Geerlof A, Li X, Cronan JE, Kaufmann SH, Wilmanns M, Proc Natl Acad Sci U S A. 2006 Jun 6;103(23):8662-7. Epub 2006 May 30. PMID:16735476
Page seeded by OCA on Mon Mar 31 00:31:47 2008
Categories: Mycobacterium tuberculosis | Single protein | Ma, Q. | Wilmanns, M. | XMTB, Mycobacterium Tuberculosis Structural Proteomics Project. | Acyltransferase | Lipoate-protein ligase b | Lipoic acid | Lipoyltransferase | Mycobacterium tuberculosis structural proteomics project | Structural genomic | Transferase | Xmtb
