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| - | [[Image:1l7p.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1l7p| PDB=1l7p | SCENE= }} | | {{STRUCTURE_1l7p| PDB=1l7p | SCENE= }} |
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| - | '''SUBSTRATE BOUND PHOSPHOSERINE PHOSPHATASE COMPLEX STRUCTURE'''
| + | ===SUBSTRATE BOUND PHOSPHOSERINE PHOSPHATASE COMPLEX STRUCTURE=== |
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| - | ==Overview==
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| - | Phosphoserine phosphatase (PSP) is a member of a large class of enzymes that catalyze phosphoester hydrolysis using a phosphoaspartate-enzyme intermediate. PSP is a likely regulator of the steady-state d-serine level in the brain, which is a critical co-agonist of the N-methyl-d-aspartate type of glutamate receptors. Here, we present high-resolution (1.5-1.9 A) structures of PSP from Methanococcus jannaschii, which define the open state prior to substrate binding, the complex with phosphoserine substrate bound (with a D to N mutation in the active site), and the complex with AlF3, a transition-state analog for the phospho-transfer steps in the reaction. These structures, together with those described for the BeF3- complex (mimicking the phospho-enzyme) and the enzyme with phosphate product in the active site, provide a detailed structural picture of the full reaction cycle. The structure of the apo state indicates partial unfolding of the enzyme to allow substrate binding, with refolding in the presence of substrate to provide specificity. Interdomain and active-site conformational changes are identified. The structure with the transition state analog bound indicates a "tight" intermediate. A striking structure homology, with significant sequence conservation, among PSP, P-type ATPases and response regulators suggests that the knowledge of the PSP reaction mechanism from the structures determined will provide insights into the reaction mechanisms of the other enzymes in this family.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12051918}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12051918 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12051918}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rossmann fold]] | | [[Category: Rossmann fold]] |
| | [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:38:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:53:32 2008'' |
Revision as of 08:53, 2 July 2008
Template:STRUCTURE 1l7p
SUBSTRATE BOUND PHOSPHOSERINE PHOSPHATASE COMPLEX STRUCTURE
Template:ABSTRACT PUBMED 12051918
About this Structure
1L7P is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states., Wang W, Cho HS, Kim R, Jancarik J, Yokota H, Nguyen HH, Grigoriev IV, Wemmer DE, Kim SH, J Mol Biol. 2002 May 31;319(2):421-31. PMID:12051918
Page seeded by OCA on Wed Jul 2 11:53:32 2008
Categories: Methanocaldococcus jannaschii | Phosphoserine phosphatase | Single protein | BSGC, Berkeley Structural Genomics Center. | Cho, H S. | Grigoriev, I V. | Jancarik, J. | Kim, R. | Kim, S H. | Nguyen, H H. | Wang, W. | Wemmer, D E. | Yokota, H. | Berkeley structural genomics center | Beta-hairpin | Bsgc structure funded by nih | Four-helix bundle | Protein structure initiative | Psi | Rossmann fold | Structural genomic