This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1qgx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qgx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1qgx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qgx| PDB=1qgx | SCENE= }}
{{STRUCTURE_1qgx| PDB=1qgx | SCENE= }}
-
'''X-RAY STRUCTURE OF YEAST HAL2P'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10656801}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10656801 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10656801}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Nucleotidase]]
[[Category: Nucleotidase]]
[[Category: Salt tollerance]]
[[Category: Salt tollerance]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:15:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:03:54 2008''

Revision as of 02:03, 28 July 2008

Image:1qgx.png

Template:STRUCTURE 1qgx

X-RAY STRUCTURE OF YEAST HAL2P

Template:ABSTRACT PUBMED 10656801

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

Page seeded by OCA on Mon Jul 28 05:03:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qgx"
Personal tools