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2oda

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{{STRUCTURE_2oda| PDB=2oda | SCENE= }}
{{STRUCTURE_2oda| PDB=2oda | SCENE= }}
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'''Crystal Structure of PSPTO_2114'''
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===Crystal Structure of PSPTO_2114===
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==Overview==
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The haloacid dehalogenase (HAD) superfamily is a large family of proteins dominated by phosphotransferases. Thirty-three sequence families within the HAD superfamily (HADSF) have been identified to assist in function assignment. One such family includes the enzyme phosphoacetaldehyde hydrolase (phosphonatase). Phosphonatase possesses the conserved Rossmanniod core domain and a C1-type cap domain. Other members of this family do not possess a cap domain and because the cap domain of phosphonatase plays an important role in active site desolvation and catalysis, the function of the capless family members must be unique. A representative of the capless subfamily, PSPTO_2114, from the plant pathogen Pseudomonas syringae, was targeted for catalytic activity and structure analyses. The X-ray structure of PSPTO_2114 reveals a capless homodimer that conserves some but not all of the intersubunit contacts contributed by the core domains of the phosphonatase homodimer. The region of the PSPTO_2114 that corresponds to the catalytic scaffold of phosphonatase (and other HAD phosphotransfereases) positions amino acid residues that are ill suited for Mg+2 cofactor binding and mediation of phosphoryl group transfer between donor and acceptor substrates. The absence of phosphotransferase activity in PSPTO_2114 was confirmed by kinetic assays. To explore PSPTO_2114 function, the conservation of sequence motifs extending outside of the HADSF catalytic scaffold was examined. The stringently conserved residues among PSPTO_2114 homologs were mapped onto the PSPTO_2114 three-dimensional structure to identify a surface region unique to the family members that do not possess a cap domain. The hypothesis that this region is used in protein-protein recognition is explored to define, for the first time, HADSF proteins which have acquired a function other than that of a catalyst.
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(as it appears on PubMed at http://www.pubmed.gov), where 17654544 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17654544}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The X-ray crystallographic structure and activity analysis of a Pseudomonas-specific subfamily of the HAD enzyme superfamily evidences a novel biochemical function., Peisach E, Wang L, Burroughs AM, Aravind L, Dunaway-Mariano D, Allen KN, Proteins. 2008 Jan 1;70(1):197-207. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17654544 17654544]
The X-ray crystallographic structure and activity analysis of a Pseudomonas-specific subfamily of the HAD enzyme superfamily evidences a novel biochemical function., Peisach E, Wang L, Burroughs AM, Aravind L, Dunaway-Mariano D, Allen KN, Proteins. 2008 Jan 1;70(1):197-207. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17654544 17654544]
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The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily., Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN, Biochemistry. 2000 Aug 29;39(34):10385-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10956028 10956028]
[[Category: Pseudomonas syringae pv. tomato]]
[[Category: Pseudomonas syringae pv. tomato]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Phosphonoacetaldehyde hydrolase]]
[[Category: Phosphonoacetaldehyde hydrolase]]
[[Category: Protein binding]]
[[Category: Protein binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:39:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:55:30 2008''

Revision as of 10:55, 28 July 2008

Image:2oda.png

Template:STRUCTURE 2oda

Crystal Structure of PSPTO_2114

Template:ABSTRACT PUBMED 17654544

About this Structure

2ODA is a Single protein structure of sequence from Pseudomonas syringae pv. tomato. Full crystallographic information is available from OCA.

Reference

The X-ray crystallographic structure and activity analysis of a Pseudomonas-specific subfamily of the HAD enzyme superfamily evidences a novel biochemical function., Peisach E, Wang L, Burroughs AM, Aravind L, Dunaway-Mariano D, Allen KN, Proteins. 2008 Jan 1;70(1):197-207. PMID:17654544

The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily., Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN, Biochemistry. 2000 Aug 29;39(34):10385-96. PMID:10956028

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