1cq7
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| , resolution 2.4Å | |||||||
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| Ligands: | |||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||
| Related: | 1C9C, 1CQ6, 1CQ8
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ASPARTATE AMINOTRANSFERASE (E.C. 2.6.1.1) COMPLEXED WITH C5-PYRIDOXAL-5P-PHOSPHATE
OverviewOverview
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.
About this StructureAbout this Structure
1CQ7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Free energy requirement for domain movement of an enzyme., Ishijima J, Nakai T, Kawaguchi S, Hirotsu K, Kuramitsu S, J Biol Chem. 2000 Jun 23;275(25):18939-45. PMID:10858450
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