1rkv | pdb_00001rkv
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Structure of Phosphate complex of ThrH from Pseudomonas aeruginosa
Overview
The thrH gene product of Pseudomonas aeruginosa has been shown to, complement both homoserine kinase (thrB gene product) and phosphoserine, phosphatase (serB gene product) activities in vivo. Sequence comparison, has revealed that ThrH is related to phosphoserine phosphatases (PSP, EC, 3.1.3.3) and belongs to the l-2-haloacid dehalogenase-like protein, superfamily. We have solved the crystal structures of ThrH in the apoform, and in complex with a bound product phosphate. The structure confirms an, overall fold similar to that of PSP. Most of the catalytic residues of PSP, are also conserved in ThrH, suggesting that similar catalytic mechanisms, are used by both enzymes. Spectrophotometry-based in vitro assays show, that ThrH is indeed a phosphoserine phosphatase with a K(m) of 0.207 mm, and k(cat) of 13.4 min(-1), comparable with those of other PSPs. More, interestingly, using high pressure liquid chromatography-based assays, we, have demonstrated that ThrH is able to further transfer the phosphoryl, group to homoserine using phosphoserine as the phosphoryl group donor, indicating that ThrH has a novel phosphoserine:homoserine, phosphotransferase activity.
About this Structure
1RKV is a Single protein structure of sequence from Pseudomonas aeruginosa pao1 with PO4, MG and EDO as ligands. Full crystallographic information is available from OCA.
Reference
The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activity., Singh SK, Yang K, Karthikeyan S, Huynh T, Zhang X, Phillips MA, Zhang H, J Biol Chem. 2004 Mar 26;279(13):13166-73. Epub 2003 Dec 29. PMID:14699121
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