1C9C
ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE
Summary for 1C9C
| Entry DOI | 10.2210/pdb1c9c/pdb |
| Related | 1CQ6 1CQ7 1CQ8 |
| Descriptor | ASPARTATE AMINOTRANSFERASE, ALANYL-PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | enzyme-substrate complex, transferase |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm: P00509 |
| Total number of polymer chains | 1 |
| Total formula weight | 43939.45 |
| Authors | Ishijima, J.,Nakai, T.,Kawaguchi, S.,Hirotsu, K.,Kuramitsu, S. (deposition date: 1999-08-02, release date: 2000-12-20, Last modification date: 2024-02-07) |
| Primary citation | Ishijima, J.,Nakai, T.,Kawaguchi, S.,Hirotsu, K.,Kuramitsu, S. Free energy requirement for domain movement of an enzyme J.Biol.Chem., 275:18939-18945, 2000 Cited by PubMed Abstract: Domain movement is sometimes essential for substrate recognition by an enzyme. X-ray crystallography of aminotransferase with a series of aliphatic substrates showed that the domain movement of aspartate aminotransferase was changed dramatically from an open to a closed form by the addition of only one CH(2) to the side chain of the C4 substrate CH(3)(CH(2))C((alpha))H(NH(3)(+))COO(-). These crystallographic results and reaction kinetics (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63; Kawaguchi, S. and Kuramitsu, S. (1998) J. Biol. Chem. 273, 18353-18364) enabled us to estimate the free energy required for the domain movement. PubMed: 10858450DOI: 10.1074/jbc.275.25.18939 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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