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  The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase

Ma, Q., Zhao, X., Nasser Eddine, A., Geerlof, A., Li, X., Cronan, J. E., et al. (2006). The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase. Proceedings of the National Academy of Sciences of the United States of America, 103(23), 8662-8667.

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Genre: Zeitschriftenartikel
Alternativer Titel : Proc. Natl. Acad. Sci. U. S. A.

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 Urheber:
Ma, Qingjun, Autor
Zhao, Xin, Autor
Nasser Eddine, Ali1, Autor           
Geerlof, Arie, Autor
Li, Xinping, Autor
Cronan, John E., Autor
Kaufmann, Stefan H. E.1, Autor           
Wilmanns, Matthias, Autor
Affiliations:
1Department of Immunology, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664146              

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Schlagwörter: catalytic dyad; lipoic acid; x-ray structure; thioester formation; mass spectrometry
 Zusammenfassung: 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.

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Sprache(n): eng - English
 Datum: 2006-06-06
 Publikationsstatus: Erschienen
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 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 300454
ISI: 000238278400017
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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Alternativer Titel : Proc. Natl. Acad. Sci. U. S. A.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 103 (23) Artikelnummer: - Start- / Endseite: 8662 - 8667 Identifikator: ISSN: 0027-8424