1VA4

Pseudomonas fluorescens aryl esterase

Summary for 1VA4

• Entry DOI: 10.2210/pdb1va4/pdb
• Descriptor: Arylesterase, GLYCEROL (3 entities in total)
• Functional Keywords: alpha/beta hydrolase, esterase, non-cofactor dependent haloperoxidase, hydrolase
• Biological source: Pseudomonas fluorescens
• Total number of polymer chains: 6
• Total formula weight: 187643.61

Authors

Cheeseman, J.D.,Tocilj, A.,Park, S.,Schrag, J.D.,Kazlauskas, R.J. (deposition date: 2004-02-11, release date: 2004-07-06, Last modification date: 2023-10-25)

Primary citation

Cheeseman, J.D.,Tocilj, A.,Park, S.,Schrag, J.D.,Kazlauskas, R.J.
Structure of an aryl esterase from Pseudomonas fluorescens.
Acta Crystallogr.,Sect.D, 60:1237-1243, 2004

PubMed Abstract: 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.

PubMed: 15213385
DOI: 10.1107/S0907444904010522

Experimental method

X-RAY DIFFRACTION (1.804 Å)