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1w66
From Proteopedia
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[[Image:1w66.gif|left|200px]] | [[Image:1w66.gif|left|200px]] | ||
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'''STRUCTURE OF A LIPOATE-PROTEIN LIGASE B FROM MYCOBACTERIUM TUBERCULOSIS''' | '''STRUCTURE OF A LIPOATE-PROTEIN LIGASE B FROM MYCOBACTERIUM TUBERCULOSIS''' | ||
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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: | + | [[Category: Acyltransferase]] |
| - | [[Category: | + | [[Category: Lipoate-protein ligase b]] |
| - | [[Category: | + | [[Category: Lipoic acid]] |
| - | [[Category: | + | [[Category: Lipoyltransferase]] |
| - | [[Category: | + | [[Category: Mycobacterium tuberculosis structural proteomics project]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | [[Category: | + | [[Category: Xmtb]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:12:45 2008'' | |
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Revision as of 10:12, 3 May 2008
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 Sat May 3 13:12:45 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
