2qb7
From Proteopedia
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|PDB= 2qb7 |SIZE=350|CAPTION= <scene name='initialview01'>2qb7</scene>, resolution 1.60Å | |PDB= 2qb7 |SIZE=350|CAPTION= <scene name='initialview01'>2qb7</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Exopolyphosphatase Exopolyphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.11 3.6.1.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Exopolyphosphatase Exopolyphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.11 3.6.1.11] </span> |
|GENE= PPX1, YHR201C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= PPX1, YHR201C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2qb6|2QB6]], [[2qb8|2QB8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qb7 OCA], [http://www.ebi.ac.uk/pdbsum/2qb7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qb7 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ugochukwu, E.]] | [[Category: Ugochukwu, E.]] | ||
[[Category: White, S A.]] | [[Category: White, S A.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CO]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: PO4]] | ||
[[Category: a/b/a structure]] | [[Category: a/b/a structure]] | ||
[[Category: dhh family phosphatase]] | [[Category: dhh family phosphatase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:47:13 2008'' |
Revision as of 01:47, 31 March 2008
| |||||||
| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | PPX1, YHR201C (Saccharomyces cerevisiae) | ||||||
| Activity: | Exopolyphosphatase, with EC number 3.6.1.11 | ||||||
| Related: | 2QB6, 2QB8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Saccharomyces cerevisiae cytosolic exopolyphosphatase, phosphate complex
Overview
Inorganic long-chain polyphosphate is a ubiquitous linear polymer in biology, consisting of many phosphate moieties linked by phosphoanhydride bonds. It is synthesized by polyphosphate kinase, and metabolised by a number of enzymes, including exo- and endopolyphosphatases. The Saccharomyces cerevisiae gene PPX1 encodes for a 45 kDa, metal-dependent, cytosolic exopolyphosphatase that processively cleaves the terminal phosphate group from the polyphosphate chain, until inorganic pyrophosphate is all that remains. PPX1 belongs to the DHH family of phosphoesterases, which includes: family-2 inorganic pyrophosphatases, found in Gram-positive bacteria; prune, a cyclic AMPase; and RecJ, a single-stranded DNA exonuclease. We describe the high-resolution X-ray structures of yeast PPX1, solved using the multiple isomorphous replacement with anomalous scattering (MIRAS) technique, and its complexes with phosphate (1.6 A), sulphate (1.8 A) and ATP (1.9 A). Yeast PPX1 folds into two domains, and the structures reveal a strong similarity to the family-2 inorganic pyrophosphatases, particularly in the active-site region. A large, extended channel formed at the interface of the N and C-terminal domains is lined with positively charged amino acids and represents a conduit for polyphosphate and the site of phosphate hydrolysis. Structural comparisons with the inorganic pyrophosphatases and analysis of the ligand-bound complexes lead us to propose a hydrolysis mechanism. Finally, we discuss a structural basis for substrate selectivity and processivity.
About this Structure
2QB7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The crystal structure of the cytosolic exopolyphosphatase from Saccharomyces cerevisiae reveals the basis for substrate specificity., Ugochukwu E, Lovering AL, Mather OC, Young TW, White SA, J Mol Biol. 2007 Aug 24;371(4):1007-21. Epub 2007 May 31. PMID:17599355
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