1rkv
Structure of Phosphate complex of ThrH from Pseudomonas aeruginosa
Structural highlights
FunctionTHRH_PSEAE Phosphoserine phosphatase that mediates dephosphorylation of phosphoserine in the serine biosynthesis pathway. Also able to dephosphorylate other substrates such as phospho-L(or D)-threonine, with lower activity. Shows phosphoserine:homoserine phosphotransferase activity by transferring the phosphoryl group to homoserine using phosphoserine as the phosphoryl group donor.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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