1c9c
From Proteopedia
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|PDB= 1c9c |SIZE=350|CAPTION= <scene name='initialview01'>1c9c</scene>, resolution 2.4Å | |PDB= 1c9c |SIZE=350|CAPTION= <scene name='initialview01'>1c9c</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PP3:ALANYL-PYRIDOXAL-5 | + | |LIGAND= <scene name='pdbligand=PP3:ALANYL-PYRIDOXAL-5'-PHOSPHATE'>PP3</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] | ||
|GENE= | |GENE= | ||
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[[Category: enzyme-substrate complex]] | [[Category: enzyme-substrate complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:21:09 2008'' |
Revision as of 09:21, 23 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | |||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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