NMR assignment of $^2H$, $^{13}C$ and $^{15}N$ labeled amino-terminal domain of apo-pantothenate synthetase from E. coli

Chakrabarti, Kalyan Sundar and Sarma, Siddhartha P (2006) NMR assignment of $^2H$, $^{13}C$ and $^{15}N$ labeled amino-terminal domain of apo-pantothenate synthetase from E. coli. In: Journal of Biomolecular NMR, 36 (Suppl ). p. 38.

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Abstract

Pantothenate (vitamin $b_5$) is an essential precursor for the biosynthesis of coenzyme A (CoA), an essential metabolite for many important cellular processes (Brown et al., 1987). Pantothenate Synthetase (PS) catalyzes the ATP dependent condensation of D-pantoate with $_\beta$-alanine to give rise to pantothenate. Our interest lies in studying the solution-state inter-domain interactions in E. coli PS that results in formation of the catalytic site. As a first step we have cloned and over-expressed an isotopically enriched sample of the dimeric amino-terminal domain (residues 1–176) of E. coli PS. Here we report the backbone and side-chain assignments for HN, $^{13}C (C^a, C^\beta & CO)$ and $^{15}N$ nuclei of the protein, obtained using triple resonance NMR experiments (Yamazaki et al., 1994). CSI and NOE data indicates that the protein is well folded containing both \alpha-helices and $_\beta$-sheet. Assignment for \sim 95% of backbone and side-chain resonances for the catalytic domain has been obtained and deposited in BMRB (accession # 6940).

Item Type:	Journal Article
Publication:	Journal of Biomolecular NMR
Publisher:	Springer
Additional Information:	Copyright of this article belongs to Springer.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	28 Feb 2007
Last Modified:	19 Sep 2010 04:34
URI:	http://eprints.iisc.ac.in/id/eprint/9525

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