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1rku
From Proteopedia
(New page: 200px<br /><applet load="1rku" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rku, resolution 1.47Å" /> '''Crystal Structure of...) |
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| - | [[Image:1rku.jpg|left|200px]]<br /><applet load="1rku" size=" | + | [[Image:1rku.jpg|left|200px]]<br /><applet load="1rku" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rku, resolution 1.47Å" /> | caption="1rku, resolution 1.47Å" /> | ||
'''Crystal Structure of ThrH gene product of Pseudomonas Aeruginosa'''<br /> | '''Crystal Structure of ThrH gene product of Pseudomonas Aeruginosa'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The thrH gene product of Pseudomonas aeruginosa has been shown to | + | 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== | ==About this Structure== | ||
| - | 1RKU 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 MG and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RKU 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=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=1RKU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Huynh, T.]] | [[Category: Huynh, T.]] | ||
[[Category: Karthikeyan, S.]] | [[Category: Karthikeyan, S.]] | ||
| - | [[Category: Phillips, M | + | [[Category: Phillips, M A.]] |
| - | [[Category: Singh, S | + | [[Category: Singh, S K.]] |
[[Category: Subramanian, K.]] | [[Category: Subramanian, K.]] | ||
[[Category: Yang, K.]] | [[Category: Yang, K.]] | ||
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[[Category: thrh]] | [[Category: thrh]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:02 2008'' |
Revision as of 12:52, 21 February 2008
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Crystal Structure of ThrH gene product of 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
1RKU is a Single protein structure of sequence from Pseudomonas aeruginosa pao1 with and 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
Page seeded by OCA on Thu Feb 21 14:52:02 2008
Categories: Pseudomonas aeruginosa pao1 | Single protein | Huynh, T. | Karthikeyan, S. | Phillips, M A. | Singh, S K. | Subramanian, K. | Yang, K. | Zhang, H. | Zhang, X. | EDO | MG | Phosphoserine phosphatase | Phosphoserine phosphoryl donor | Phosphoserine:homoserine phosphotransferase | Structure | Thrh
