11as

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[[Image:11as.jpg|left|200px]]
[[Image:11as.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 11as |SIZE=350|CAPTION= <scene name='initialview01'>11as</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_11as", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= ASNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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-->
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|DOMAIN=
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{{STRUCTURE_11as| PDB=11as | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=11as FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=11as OCA], [http://www.ebi.ac.uk/pdbsum/11as PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=11as RCSB]</span>
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}}
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'''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE'''
'''ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE'''
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[[Category: Nakatsu, T.]]
[[Category: Nakatsu, T.]]
[[Category: Oda, J.]]
[[Category: Oda, J.]]
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[[Category: asparagine synthetase]]
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[[Category: Asparagine synthetase]]
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[[Category: ligase]]
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[[Category: Ligase]]
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[[Category: nitrogen fixation]]
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[[Category: Nitrogen fixation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:27:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:27:06 2008''
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Revision as of 06:27, 2 May 2008

Image:11as.jpg

Template:STRUCTURE 11as

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. 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 Fri May 2 09:27:12 2008

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