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| [[Image:1mjw.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1mjw| PDB=1mjw | SCENE= }} | | {{STRUCTURE_1mjw| PDB=1mjw | SCENE= }} |
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| '''STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N'''
| | ===STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N=== |
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| ==Overview==
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| The three-dimensional structures of four mutant E. coli inorganic pyrophosphatases (PPases) with single Asp-->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-->Asn and Asp-65-->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 |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9668207 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9668207}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Mutation]] | | [[Category: Mutation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:14:15 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:08:34 2008'' |
