1ekp: Difference between revisions
New page: left|200px<br /> <applet load="1ekp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ekp, resolution 2.50Å" /> '''CRYSTAL STRUCTURE O... |
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'''CRYSTAL STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 2.5 ANGSTROMS (MONOCLINIC FORM).'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 2.5 ANGSTROMS (MONOCLINIC FORM).'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1EKP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1EKP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: fold type iv]] | [[Category: fold type iv]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:43:58 2008'' | ||
Revision as of 16:43, 15 February 2008
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CRYSTAL STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 2.5 ANGSTROMS (MONOCLINIC FORM).
OverviewOverview
X-ray crystal structures of three forms of human mitochondrial, branched-chain aminotransferase (BCAT) were solved by, molecular-replacement methods, using Escherichia coli BCAT as the search, model. The enzyme is a homodimer and the polypeptide chain of each monomer, has two domains. The small domain is composed of residues 1--175 and the, large domain is composed of residues 176--365. The active site is close to, the dimer interface. The 4'-aldehyde of the PLP cofactor is covalently, linked to the epsilon-amino group of the active-site lysine, Lys202, via a, Schiff-base linkage in two of the structures. In the third structure, the, enzyme is irreversibly inactivated by Tris. The overall fold of the dimer, in human mitochondrial BCAT is similar to the structure of two bacterial, enzymes, E. coli BCAT and D-amino acid aminotransferase (D-AAT). The, residues lining the putative substrate-binding pocket of human BCAT and, D-AAT are completely rearranged to allow catalysis with substrates of, opposite stereochemistry. In the case of human mitochondrial, branched-chain aminotransferase, a hydrogen-bond interaction between the, guanidinium group of Arg143 in the first monomer with the side-chain, hydroxyl of Tyr70 in the second monomer is important in the formation of, the substrate-binding pocket.
DiseaseDisease
Known diseases associated with this structure: Hypervalinemia or hyperleucine-isoleucinemia (1) OMIM:[113530]
About this StructureAbout this Structure
1EKP is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Branched-chain-amino-acid transaminase, with EC number 2.6.1.42 Full crystallographic information is available from OCA.
ReferenceReference
The structure of human mitochondrial branched-chain aminotransferase., Yennawar N, Dunbar J, Conway M, Hutson S, Farber G, Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):506-15. PMID:11264579
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