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| {{STRUCTURE_1rkv| PDB=1rkv | SCENE= }} | | {{STRUCTURE_1rkv| PDB=1rkv | SCENE= }} |
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| '''Structure of Phosphate complex of ThrH from Pseudomonas aeruginosa'''
| | ===Structure of Phosphate complex of ThrH from Pseudomonas aeruginosa=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_14699121}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14699121 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14699121}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Structure]] | | [[Category: Structure]] |
| [[Category: Thrh]] | | [[Category: Thrh]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:37:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:31:44 2008'' |
