1ekf

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==CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM)==
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[[Image:1ekf.png|left|200px]]
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<StructureSection load='1ekf' size='340' side='right' caption='[[1ekf]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ekf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EKF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ekp|1ekp]], [[1ekv|1ekv]]</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ekf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ekf OCA], [http://pdbe.org/1ekf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ekf RCSB], [http://www.ebi.ac.uk/pdbsum/1ekf PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/BCAT2_HUMAN BCAT2_HUMAN]] Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ek/1ekf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ekf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:11264579</ref>
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The line below this paragraph, containing "STRUCTURE_1ekf", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_1ekf| PDB=1ekf | SCENE= }}
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===CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ekf" style="background-color:#fffaf0;"></div>
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==See Also==
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<!--
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*[[Aminotransferase|Aminotransferase]]
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The line below this paragraph, {{ABSTRACT_PUBMED_11264579}}, adds the Publication Abstract to the page
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== References ==
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(as it appears on PubMed at http://www.pubmed.gov), where 11264579 is the PubMed ID number.
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<references/>
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-->
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__TOC__
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{{ABSTRACT_PUBMED_11264579}}
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</StructureSection>
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==About this Structure==
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1EKF is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EKF OCA].
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==Reference==
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<ref group="xtra">PMID:11264579</ref><references group="xtra"/>
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[[Category: Branched-chain-amino-acid transaminase]]
[[Category: Branched-chain-amino-acid transaminase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Conway, M.]]
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[[Category: Conway, M]]
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[[Category: Dunbar, J H.]]
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[[Category: Dunbar, J H]]
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[[Category: Farber, G K.]]
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[[Category: Farber, G K]]
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[[Category: Hutson, S M.]]
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[[Category: Hutson, S M]]
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[[Category: Yennawar, N H.]]
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[[Category: Yennawar, N H]]
[[Category: Fold type iv]]
[[Category: Fold type iv]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:05:31 2009''
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Current revision

CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM)

1ekf, resolution 1.95Å

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