2AAT

2.8-ANGSTROMS-RESOLUTION CRYSTAL STRUCTURE OF AN ACTIVE-SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI

Summary for 2AAT

• Entry DOI: 10.2210/pdb2aat/pdb
• Descriptor: ASPARTATE AMINOTRANSFERASE, SULFATE ION, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: transferase(aminotransferase)
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P00509
• Total number of polymer chains: 1
• Total formula weight: 43905.35

Authors

Smith, D.,Almo, S.C.,Toney, M.,Ringe, D. (deposition date: 1989-05-30, release date: 1989-10-15, Last modification date: 2024-02-14)

Primary citation

Smith, D.L.,Almo, S.C.,Toney, M.D.,Ringe, D.
2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.
Biochemistry, 28:8161-8167, 1989

PubMed Abstract: The three-dimensional structure of a mutant of the aspartate aminotransferase from Escherichia coli, in which the active-site lysine has been substituted by alanine (K258A), has been determined at 2.8-A resolution by X-ray diffraction. The mutant enzyme contains pyridoxamine phosphate as cofactor. The structure is compared to that of the mitochondrial aspartate aminotransferase. The most striking differences, aside from the absence of the lysine side chain, occur in the positions of the pyridoxamine group and of tryptophan 140.

PubMed: 2513875
DOI: 10.1021/bi00446a030

Experimental method

X-RAY DIFFRACTION (2.8 Å)