1rku: Difference between revisions

Revision as of 15:11, 27 July 2008

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File:1rku.png

Template:STRUCTURE 1rku

Crystal Structure of ThrH gene product of Pseudomonas AeruginosaCrystal Structure of ThrH gene product of Pseudomonas Aeruginosa

Template:ABSTRACT PUBMED 14699121

About this StructureAbout this Structure

1RKU is a Single protein structure of sequence from Pseudomonas aeruginosa pao1. Full crystallographic information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of ThrH gene product of Pseudomonas Aeruginosa'''
+===Crystal Structure of ThrH gene product of Pseudomonas Aeruginosa===
-==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
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 ==About this Structure==
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 [[Category: Structure]]
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