1l7n

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|PDB= 1l7n |SIZE=350|CAPTION= <scene name='initialview01'>1l7n</scene>, resolution 1.8&Aring;
|PDB= 1l7n |SIZE=350|CAPTION= <scene name='initialview01'>1l7n</scene>, resolution 1.8&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=AF3:ALUMINUM FLUORIDE'>AF3</scene>
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|LIGAND= <scene name='pdbligand=AF3:ALUMINUM+FLUORIDE'>AF3</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoserine_phosphatase Phosphoserine phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.3 3.1.3.3] </span>
|GENE= MJ1594 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])
|GENE= MJ1594 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0560 SerB]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l7n OCA], [http://www.ebi.ac.uk/pdbsum/1l7n PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1l7n RCSB]</span>
}}
}}
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[[Category: Wemmer, D E.]]
[[Category: Wemmer, D E.]]
[[Category: Yokota, H.]]
[[Category: Yokota, H.]]
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[[Category: AF3]]
 
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[[Category: ALF]]
 
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[[Category: MG]]
 
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[[Category: SO4]]
 
[[Category: b-hairpin]]
[[Category: b-hairpin]]
[[Category: berkeley structural genomics center]]
[[Category: berkeley structural genomics center]]
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:27:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:55:47 2008''

Revision as of 03:55, 26 March 2008


PDB ID 1l7n

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: , , , ,
Gene: MJ1594 (Methanocaldococcus jannaschii)
Activity: Phosphoserine phosphatase, with EC number 3.1.3.3
Domains: SerB
Resources: FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates: save as pdb, mmCIF, xml



TRANSITION STATE ANALOGUE OF PHOSPHOSERINE PHOSPHATASE (ALUMINUM FLUORIDE COMPLEX)


Overview

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.

About this Structure

1L7N 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

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