1mjw: Difference between revisions
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|PDB= 1mjw |SIZE=350|CAPTION= <scene name='initialview01'>1mjw</scene>, resolution 1.95Å | |PDB= 1mjw |SIZE=350|CAPTION= <scene name='initialview01'>1mjw</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mjw OCA], [http://www.ebi.ac.uk/pdbsum/1mjw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mjw RCSB]</span> | |||
}} | }} | ||
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[[Category: Oganesyan, V.]] | [[Category: Oganesyan, V.]] | ||
[[Category: Samygina, V R.]] | [[Category: Samygina, V R.]] | ||
[[Category: acid anhydride hydrolase]] | [[Category: acid anhydride hydrolase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: mutation]] | [[Category: mutation]] | ||
''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 22:16:58 2008'' | ||
Revision as of 22:17, 30 March 2008
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| , resolution 1.95Å | |||||||
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| Ligands: | |||||||
| Activity: | Inorganic diphosphatase, with EC number 3.6.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N
OverviewOverview
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.
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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