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12as
From Proteopedia
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|PDB= 12as |SIZE=350|CAPTION= <scene name='initialview01'>12as</scene>, resolution 2.2Å | |PDB= 12as |SIZE=350|CAPTION= <scene name='initialview01'>12as</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=NU1:Amp+Binding+(Catalytic)+Site+(Chain+A).+Site+Site_identi+...'>NU1</scene> and <scene name='pdbsite=NU2:Amp+Binding+(Catalytic)+Site+(Chain+B)'>NU2</scene> | |SITE= <scene name='pdbsite=NU1:Amp+Binding+(Catalytic)+Site+(Chain+A).+Site+Site_identi+...'>NU1</scene> and <scene name='pdbsite=NU2:Amp+Binding+(Catalytic)+Site+(Chain+B)'>NU2</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= ASNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ASNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=12as FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=12as OCA], [http://www.ebi.ac.uk/pdbsum/12as PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=12as RCSB]</span> | ||
}} | }} | ||
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[[Category: Nakatsu, T.]] | [[Category: Nakatsu, T.]] | ||
[[Category: Oda, J.]] | [[Category: Oda, J.]] | ||
| - | [[Category: AMP]] | ||
| - | [[Category: ASN]] | ||
[[Category: asparagine synthetase]] | [[Category: asparagine synthetase]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
[[Category: nitrogen fixation]] | [[Category: nitrogen fixation]] | ||
| - | ''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 18:27:25 2008'' |
Revision as of 15:27, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , | ||||||
| Gene: | ASNA (Escherichia coli) | ||||||
| Activity: | Aspartate--ammonia ligase, with EC number 6.3.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP
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
12AS 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
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