2hgx

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{{Seed}}
 
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[[Image:2hgx.png|left|200px]]
 
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==Crystal structure of Cys315Ala mutant of human mitochondrial branched chain aminotransferase==
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The line below this paragraph, containing "STRUCTURE_2hgx", creates the "Structure Box" on the page.
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<StructureSection load='2hgx' size='340' side='right'caption='[[2hgx]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2hgx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HGX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <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"><div style='overflow: auto; max-height: 3em;'>[[1ekf|1ekf]], [[1ekp|1ekp]], [[1ekv|1ekv]], [[1kta|1kta]], [[1kt8|1kt8]], [[2a1h|2a1h]], [[2hdk|2hdk]], [[2hg8|2hg8]], [[2hgw|2hgw]], [[2hhf|2hhf]]</div></td></tr>
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{{STRUCTURE_2hgx| PDB=2hgx | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCAT2, BCATM, ECA40 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2hgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hgx OCA], [https://pdbe.org/2hgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hgx RCSB], [https://www.ebi.ac.uk/pdbsum/2hgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hgx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://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/hg/2hgx_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=2hgx 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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Mammalian branched chain aminotransferases (BCATs) have a unique CXXC center. Kinetic and structural studies of three CXXC center mutants (C315A, C318A, and C315A/C318A) of human mitochondrial (hBCATm) isozyme and the oxidized hBCATm enzyme (hBCATm-Ox) have been used to elucidate the role of this center in hBCATm catalysis. X-ray crystallography revealed that the CXXC motif, through its network of hydrogen bonds, plays a crucial role in orienting the substrate optimally for catalysis. In all structures, there were changes in the structure of the beta-turn preceding the CXXC motif when compared with wild type protein. The N-terminal loop between residues 15 and 32 is flexible in the oxidized and mutant enzymes, the disorder greater in the oxidized protein. Disordering of the N-terminal loop disrupts the integrity of the side chain binding pocket, particularly for the branched chain side chain, less so for the dicarboxylate substrate side chain. The kinetic studies of the mutant and oxidized enzymes support the structural analysis. The kinetic results showed that the predominant effect of oxidation was on the second half-reaction rather than the first half-reaction. The oxidized enzyme was completely inactive, whereas the mutants showed limited activity. Model building of the second half-reaction substrate alpha-ketoisocaproate in the pyridoxamine 5'-phosphate-hBCATm structure suggests that disruption of the CXXC center results in altered substrate orientation and deprotonation of the amino group of pyridoxamine 5'-phosphate, which inhibits catalysis.
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===Crystal structure of Cys315Ala mutant of human mitochondrial branched chain aminotransferase===
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Human mitochondrial branched chain aminotransferase isozyme: structural role of the CXXC center in catalysis.,Yennawar NH, Islam MM, Conway M, Wallin R, Hutson SM J Biol Chem. 2006 Dec 22;281(51):39660-71. Epub 2006 Oct 18. PMID:17050531<ref>PMID:17050531</ref>
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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 2hgx" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17050531}}, adds the Publication Abstract to the page
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17050531 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17050531}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2HGX 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=2HGX OCA].
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==Reference==
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<ref group="xtra">PMID:17050531</ref><ref group="xtra">PMID:9478945</ref><ref group="xtra">PMID:9165094</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: Hutson, S M.]]
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[[Category: Large Structures]]
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[[Category: Yennawar, N H.]]
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[[Category: Hutson, S M]]
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[[Category: Yennawar, N H]]
[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]
[[Category: D-aminoacid aminotransferase-like plp-dependent enzyme]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:08:57 2009''
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Current revision

Crystal structure of Cys315Ala mutant of human mitochondrial branched chain aminotransferase

PDB ID 2hgx

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