Structural highlights
Function
[ACP_BORBU] Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein was chosen as a potential target for drug-discovery efforts because of its involvement in fatty-acid biosynthesis, an essential metabolic pathway, in bacteria. It was possible to assign >98% of backbone resonances and >92% of side-chain resonances using multidimensional NMR spectroscopy. The NMR structure was determined to a backbone r.m.s.d. of 0.4 A and contained four alpha-helices and two 3(10)-helices. A structure-homology search revealed that this protein is highly similar to the acyl-carrier protein from Aquifex aeolicus.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.,Barnwal RP, Van Voorhis WC, Varani G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1137-40. Epub 2011 Aug 13. PMID:21904063[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Barnwal RP, Van Voorhis WC, Varani G. NMR structure of an acyl-carrier protein from Borrelia burgdorferi. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1137-40. Epub 2011 Aug 13. PMID:21904063 doi:10.1107/S1744309111004386
