11AS

ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE

Summary for 11AS

• Entry DOI: 10.2210/pdb11as/pdb
• Descriptor: ASPARAGINE SYNTHETASE, ASPARAGINE (3 entities in total)
• Functional Keywords: ligase, asparagine synthetase, nitrogen fixation
• Biological source: Escherichia coli K12
• Cellular location: Cytoplasm: P00963
• Total number of polymer chains: 2
• Total formula weight: 73530.97

Authors

Nakatsu, T.,Kato, H.,Oda, J. (deposition date: 1997-12-02, release date: 1998-12-30, Last modification date: 2024-03-13)

Primary citation

Nakatsu, T.,Kato, H.,Oda, J.
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase.
Nat.Struct.Biol., 5:15-19, 1998

PubMed Abstract: 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.

PubMed: 9437423
DOI: 10.1038/nsb0198-15

Experimental method

X-RAY DIFFRACTION (2.5 Å)