1a3g
From Proteopedia
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| - | [[Image:1a3g.gif|left|200px]] | + | [[Image:1a3g.gif|left|200px]] |
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| - | '''BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1a3g |SIZE=350|CAPTION= <scene name='initialview01'>1a3g</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A3G is a [ | + | 1A3G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3G OCA]. |
==Reference== | ==Reference== | ||
| - | Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution., Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H, J Biochem. 1997 Apr;121(4):637-41. PMID:[http:// | + | Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution., Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H, J Biochem. 1997 Apr;121(4):637-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9163511 9163511] |
[[Category: Branched-chain-amino-acid transaminase]] | [[Category: Branched-chain-amino-acid transaminase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: pyridoxal enzyme]] | [[Category: pyridoxal enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:52:19 2008'' |
Revision as of 07:52, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Activity: | Branched-chain-amino-acid transaminase, with EC number 2.6.1.42 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI
Overview
The X-ray crystallographic structure of the branched-chain amino acid aminotransferase from Escherichia coli was determined by means of isomorphous replacement using the selenomethionyl enzyme as one of the heavy atom derivatives. The enzyme is a homo hexamer with D3 symmetry, and the polypeptide chain of the subunit is folded into two domains (small and large domains). The coenzyme, pyridoxal 5'-phosphate, resides at the domain interface, its re-face facing toward the protein. The active site structure shows that the following sites can recognize branched-chain amino acids and glutamate as substrates: (1) a hydrophobic core formed by Phe36, Tyr164, Tyr31*, and Val109* for a branched-chain; (2) Arg97 for an acidic side chain of glutamate; and (3) Tyr95 and two main chain NH groups of Thr257 and Ala258 for the alpha-carboxylate of substrates. Although the main chain conformation of the active site is homologous to that of D-amino acid aminotransferase, many of the active site residues are different between them.
About this Structure
1A3G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution., Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H, J Biochem. 1997 Apr;121(4):637-41. PMID:9163511
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