11as
From Proteopedia
(New page: 200px<br /><applet load="11as" size="450" color="white" frame="true" align="right" spinBox="true" caption="11as, resolution 2.5Å" /> '''ASPARAGINE SYNTHETASE...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:11as.jpg|left|200px]]<br /><applet load="11as" size=" | + | [[Image:11as.jpg|left|200px]]<br /><applet load="11as" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="11as, resolution 2.5Å" /> | caption="11as, resolution 2.5Å" /> | ||
'''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE'''<br /> | '''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of E. coli asparagine synthetase has been determined | + | The crystal structure of E. coli asparagine synthetase has been determined by X-ray diffraction analysis at 2.5 A resolution. The overall structure of the enzyme is remarkably similar to that of the catalytic domain of yeast aspartyl-tRNA synthetase despite low sequence similarity. These enzymes have a common reaction mechanism that implies the formation of an aminoacyl-adenylate intermediate. The active site architecture and most of the catalytic residues are also conserved in both enzymes. These proteins have probably evolved from a common ancestor even though their sequence similarities are small. The functional and structural similarities of both enzymes suggest that new enzymatic activities would generally follow the recruitment of a protein catalyzing a similar chemical reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 11AS 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 ASN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate--ammonia_ligase Aspartate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.1 6.3.1.1] Full crystallographic information is available from [http:// | + | 11AS 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=ASN:'>ASN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aspartate--ammonia_ligase Aspartate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.1 6.3.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=11AS OCA]. |
==Reference== | ==Reference== | ||
| Line 22: | Line 22: | ||
[[Category: nitrogen fixation]] | [[Category: nitrogen fixation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:37:42 2008'' |
Revision as of 09:37, 21 February 2008
|
ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE
Overview
The crystal structure of E. coli asparagine synthetase has been determined by X-ray diffraction analysis at 2.5 A resolution. The overall structure of the enzyme is remarkably similar to that of the catalytic domain of yeast aspartyl-tRNA synthetase despite low sequence similarity. These enzymes have a common reaction mechanism that implies the formation of an aminoacyl-adenylate intermediate. The active site architecture and most of the catalytic residues are also conserved in both enzymes. These proteins have probably evolved from a common ancestor even though their sequence similarities are small. The functional and structural similarities of both enzymes suggest that new enzymatic activities would generally follow the recruitment of a protein catalyzing a similar chemical reaction.
About this Structure
11AS is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Aspartate--ammonia ligase, with EC number 6.3.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase., Nakatsu T, Kato H, Oda J, Nat Struct Biol. 1998 Jan;5(1):15-9. PMID:9437423
Page seeded by OCA on Thu Feb 21 11:37:42 2008
