1byr
From Proteopedia
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[[Category: phosphodiesterase]] | [[Category: phosphodiesterase]] | ||
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Revision as of 12:53, 30 October 2007
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CRYSTAL STRUCTURE OF A PHOSPHOLIPASE D FAMILY MEMBER, NUC FROM SALMONELLA TYPHIMURIUM
Overview
The first crystal structure of a phospholipase D (PLD) family member has, been determined at 2.0 A resolution. The PLD superfamily is defined by a, common sequence motif, HxK(x)4D(x)6GSxN, and includes enzymes involved in, signal transduction, lipid biosynthesis, endonucleases and open reading, frames in pathogenic viruses and bacteria. The crystal structure suggests, that residues from two sequence motifs form a single active site. A, histidine residue from one motif acts as a nucleophile in the catalytic, mechanism, forming a phosphoenzyme intermediate, whereas a histidine, residue from the other motif appears to function as a general acid in the, cleavage of the phosphodiester bond. The structure suggests that the, conserved lysine residues are involved in phosphate binding. ... [(full description)]
About this Structure
1BYR is a [Single protein] structure of sequence from [Salmonella typhimurium]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a phospholipase D family member., Stuckey JA, Dixon JE, Nat Struct Biol. 1999 Mar;6(3):278-84. PMID:10074947
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