1mjw: Difference between revisions

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[[Image:1mjw.gif|left|200px]]
[[Image:1mjw.gif|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_1mjw", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
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|DOMAIN=
{{STRUCTURE_1mjw| PDB=1mjw  | SCENE= }}  
|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>
}}


'''STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N'''
'''STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N'''
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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]]
 
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Revision as of 01:14, 3 May 2008

File:1mjw.gif

Template:STRUCTURE 1mjw

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 Page seeded by OCA on Sat May 3 01:14:15 2008

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