2gv1
From Proteopedia
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NMR solution structure of the Acylphosphatase from Eschaerichia Coli
Overview
The solution structure of Escherichia coli acylphosphatase (E. coli AcP), a small enzyme catalyzing the hydrolysis of acylphosphates, was determined by (1)H and (15)N NMR and restrained modelling calculation. In analogy with the other members of AcP family, E. coli AcP shows an alpha/beta sandwich domain composed of four antiparallel and one parallel beta-strand, assembled in a five-stranded beta-sheet facing two antiparallel alpha-helices. The pairwise RMSD values calculated for the backbone atoms of E. coli and Sulfolobus solfataricus AcP, Bovine common type AcP and Horse muscle AcP are 2.18, 5.31 and 5.12 A, respectively. No significant differences are present in the active site region and the catalytic residue side chains are consistently positioned in the structures.
About this Structure
2GV1 is a Single protein structure of sequence from Escherichia coli. Active as Acylphosphatase, with EC number 3.6.1.7 Full crystallographic information is available from OCA.
Reference
NMR solution structure of the acylphosphatase from Escherichia coli., Pagano K, Ramazzotti M, Viglino P, Esposito G, Degl'Innocenti D, Taddei N, Corazza A, J Biomol NMR. 2006 Nov;36(3):199-204. Epub 2006 Oct 5. PMID:17021943
Page seeded by OCA on Thu Feb 21 17:35:38 2008
