1rkv: Difference between revisions

Revision as of 15:51, 21 February 2008

Structure of Phosphate complex of ThrH from Pseudomonas aeruginosa

OverviewOverview

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 StructureAbout this Structure

1RKV is a Single protein structure of sequence from Pseudomonas aeruginosa pao1 with , and as ligands. 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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OCA

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-[[Image:1rkv.jpg|left|200px]]<br /><applet load="1rkv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rkv.jpg|left|200px]]<br /><applet load="1rkv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rkv, resolution 1.90&Aring;" />
 '''Structure of Phosphate complex of ThrH from Pseudomonas aeruginosa'''<br />
 ==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.
+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==
-RKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1] with PO4, MG and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RKV OCA].
+RKV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_pao1 Pseudomonas aeruginosa pao1] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKV OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Huynh, T.]]
 [[Category: Karthikeyan, S.]]
-[[Category: Phillips, M.A.]]
+[[Category: Phillips, M A.]]
-[[Category: Singh, S.K.]]
+[[Category: Singh, S K.]]
 [[Category: Subramanian, K.]]
 [[Category: Yang, K.]]
@@ Line 30: / Line 30: @@
 [[Category: thrh]]
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