1mjw: Difference between revisions

Revision as of 00:08, 3 July 2008

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File:1mjw.png

Template:STRUCTURE 1mjw

STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42NSTRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N

Template:ABSTRACT PUBMED 9668207

About this StructureAbout this Structure

1MJW is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structures of mutant forms of E. coli inorganic pyrophosphatase with Asp-->Asn single substitution in positions 42, 65, 70, and 97., Avaeva SM, Rodina EV, Vorobyeva NN, Kurilova SA, Nazarova TI, Sklyankina VA, Oganessyan VY, Samygina VR, Harutyunyan EH, Biochemistry (Mosc). 1998 Jun;63(6):671-84. PMID:9668207

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OCA

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-'''STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N'''
+===STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N===
-==Overview==
+<!--
-The three-dimensional structures of four mutant E. coli inorganic pyrophosphatases (PPases) with single Asp--&gt;Asn substitutions at positions 42, 65, 70, and 97 were solved at 1.95, 2.15, 2.10, and 2.20 A resolution, respectively. Asp-42--&gt;Asn and Asp-65--&gt;Asn mutant PPases were prepared as complexes with sulfate--a structural analog of phosphate, the product of enzymatic reaction. A comparison of mutant enzymes with native PPases revealed that a single amino acid substitution changes the position of the mutated residue as well as the positions of several functional groups and some parts of a polypeptide chain. These changes are responsible for the fact that mutant PPases differ from the native ones in their catalytic properties. The sulfate binding to the mutant PPase active site causes molecular asymmetry, as shown for the native PPase earlier. The subunit asymmetry is manifested in different positions of sulfate and several functional groups, as well as changes in packing of hexamers in crystals and in cell parameters.
+The line below this paragraph, {{ABSTRACT_PUBMED_9668207}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9668207}}
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 [[Category: Hydrolase]]
 [[Category: Mutation]]
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