1qgx
From Proteopedia
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|PDB= 1qgx |SIZE=350|CAPTION= <scene name='initialview01'>1qgx</scene>, resolution 1.6Å | |PDB= 1qgx |SIZE=350|CAPTION= <scene name='initialview01'>1qgx</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/3'(2'),5'-bisphosphate_nucleotidase 3'(2'),5'-bisphosphate nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.7 3.1.3.7] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3'(2'),5'-bisphosphate_nucleotidase 3'(2'),5'-bisphosphate nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.7 3.1.3.7] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgx OCA], [http://www.ebi.ac.uk/pdbsum/1qgx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qgx RCSB]</span> | ||
}} | }} | ||
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[[Category: Serrano, R.]] | [[Category: Serrano, R.]] | ||
[[Category: Yenush, L.]] | [[Category: Yenush, L.]] | ||
| - | [[Category: AMP]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: SO4]] | ||
[[Category: inositol]] | [[Category: inositol]] | ||
[[Category: nucleotidase]] | [[Category: nucleotidase]] | ||
[[Category: salt tollerance]] | [[Category: salt tollerance]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:13:24 2008'' |
Revision as of 20:13, 30 March 2008
| |||||||
| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Activity: | 3'(2'),5'-bisphosphate nucleotidase, with EC number 3.1.3.7 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY STRUCTURE OF YEAST HAL2P
Overview
The product of the yeast HAL2 gene (Hal2p) is an in vivo target of sodium and lithium toxicity and its overexpression improves salt tolerance in yeast and plants. Hal2p is a metabolic phosphatase which catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. It is, the prototype of an evolutionarily conserved family of PAP phosphatases and the engineering of sodium insensitive enzymes of this group may contribute to the generation of salt-tolerant crops. We have solved the crystal structure of Hal2p in complex with magnesium, lithium and the two products of PAP hydrolysis, AMP and Pi, at 1.6 A resolution. A functional screening of random mutations of the HAL2 gene in growing yeast generated forms of the enzyme with reduced cation sensitivity. Analysis of these mutants defined a salt bridge (Glu238 ellipsis Arg152) and a hydrophobic bond (Va170 ellipsis Trp293) as important framework interactions determining cation sensitivity. Hal2p belongs to a larger superfamily of lithium-sensitive phosphatases which includes inositol monophosphatase. The hydrophobic interaction mutated in Hal2p is conserved in this superfamily and its disruption in human inositol monophosphatase also resulted in reduced cation sensitivity.
About this Structure
1QGX is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity., Albert A, Yenush L, Gil-Mascarell MR, Rodriguez PL, Patel S, Martinez-Ripoll M, Blundell TL, Serrano R, J Mol Biol. 2000 Jan 28;295(4):927-38. PMID:10656801
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