1va4 | pdb_00001va4
Pseudomonas fluorescens aryl esterase
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Overview
The structure of PFE, an aryl esterase from Pseudomonas fluorescens, has, been solved to a resolution of 1.8 A by X-ray diffraction and shows a, characteristic alpha/beta-hydrolase fold. In addition to catalyzing the, hydrolysis of esters in vitro, PFE also shows low bromoperoxidase, activity. PFE shows highest structural similarity, including the, active-site environment, to a family of non-heme bacterial, haloperoxidases, with an r.m.s. deviation in 271 C(alpha) atoms between, PFE and its five closest structural neighbors averaging 0.8 A. PFE has far, less similarity (r.m.s. deviation in 218 C(alpha) atoms of 5.0 A) to P., fluorescens carboxyl esterase. PFE favors activated esters with small acyl, groups, such as phenyl acetate. The X-ray structure of PFE reveals a, significantly occluded active site. In addition, several residues, including Trp28 and Met95, limit the size of the acyl-binding pocket, explaining its preference for small acyl groups.
About this Structure
1VA4 is a Single protein structure of sequence from Pseudomonas fluorescens with GOL as ligand. Active as Arylesterase, with EC number 3.1.1.2 Full crystallographic information is available from OCA.
Reference
Structure of an aryl esterase from Pseudomonas fluorescens., Cheeseman JD, Tocilj A, Park S, Schrag JD, Kazlauskas RJ, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1237-43. Epub 2004, Jun 22. PMID:15213385
Page seeded by OCA on Wed Nov 21 04:32:29 2007
