1qgx

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(New page: 200px<br /><applet load="1qgx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qgx, resolution 1.6&Aring;" /> '''X-RAY STRUCTURE OF YE...)
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'''X-RAY STRUCTURE OF YEAST HAL2P'''<br />
'''X-RAY STRUCTURE OF YEAST HAL2P'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1QGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG, PO4, SO4, AMP and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QGX OCA].
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1QGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGX OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Albert, A.]]
[[Category: Albert, A.]]
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[[Category: Blundell, T.L.]]
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[[Category: Blundell, T L.]]
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[[Category: Gil-Mascarell, M.R.]]
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[[Category: Gil-Mascarell, M R.]]
[[Category: Martinez-Ripoll, M.]]
[[Category: Martinez-Ripoll, M.]]
[[Category: Patel, J.]]
[[Category: Patel, J.]]
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[[Category: Rodriguez, P.L.]]
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[[Category: Rodriguez, P L.]]
[[Category: Serrano, R.]]
[[Category: Serrano, R.]]
[[Category: Yenush, L.]]
[[Category: Yenush, L.]]
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[[Category: salt tollerance]]
[[Category: salt tollerance]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:27 2008''

Revision as of 12:39, 21 February 2008


1qgx, resolution 1.6Å

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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 with , , , and as ligands. Active as 3'(2'),5'-bisphosphate nucleotidase, with EC number 3.1.3.7 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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