1c9c
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(New page: 200px<br /><applet load="1c9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c9c, resolution 2.4Å" /> '''ASPARTATE AMINOTRANSF...)
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Revision as of 10:09, 20 November 2007
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ASPARTATE AMINOTRANSFERASE COMPLEXED WITH C3-PYRIDOXAL-5'-PHOSPHATE
Overview
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 Structure
1C9C is a Single protein structure of sequence from Escherichia coli with PP3 as ligand. Active as Aspartate transaminase, with EC number 2.6.1.1 Full crystallographic information is available from OCA.
Reference
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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