1mjw
From Proteopedia
(New page: 200px<br /><applet load="1mjw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mjw, resolution 1.95Å" /> '''STRUCTURE OF INORGAN...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mjw.gif|left|200px]]<br /><applet load="1mjw" size=" | + | [[Image:1mjw.gif|left|200px]]<br /><applet load="1mjw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mjw, resolution 1.95Å" /> | caption="1mjw, resolution 1.95Å" /> | ||
'''STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N'''<br /> | '''STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structures of four mutant E. coli inorganic | + | 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 Structure== | ==About this Structure== | ||
| - | 1MJW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1MJW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJW OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Inorganic diphosphatase]] | [[Category: Inorganic diphosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Avaeva, S | + | [[Category: Avaeva, S M.]] |
| - | [[Category: Harutyunyan, E | + | [[Category: Harutyunyan, E H.]] |
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Oganesyan, V.]] | [[Category: Oganesyan, V.]] | ||
| - | [[Category: Samygina, V | + | [[Category: Samygina, V R.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: acid anhydride hydrolase]] | [[Category: acid anhydride hydrolase]] | ||
| Line 24: | Line 24: | ||
[[Category: mutation]] | [[Category: mutation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:56 2008'' |
Revision as of 11:55, 21 February 2008
|
STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N
Overview
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 Structure
1MJW is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Inorganic diphosphatase, with EC number 3.6.1.1 Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 13:55:56 2008
