3ht5
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3ht5 is ON HOLD Authors: Tremblay, L.W., Blanchard, J.S. Description: Crystal Structure of IlvE a Branched Chain Amino Acid Transaminase from Mycob...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==Crystal Structure of IlvE a Branched Chain Amino Acid Transaminase from Mycobacterium tuberculosis== |
| + | <StructureSection load='3ht5' size='340' side='right'caption='[[3ht5]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ht5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HT5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ht5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ht5 OCA], [https://pdbe.org/3ht5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ht5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ht5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ht5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ILVE_MYCTU ILVE_MYCTU] Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val.<ref>PMID:20445230</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/3ht5_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=3ht5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Unlike mammals, bacteria encode enzymes that synthesize branched-chain amino acids. The pyridoxal 50-phosphate-dependent transaminase performs the final biosynthetic step in these pathways, converting keto acid precursors into -amino acids. The branched-chain amino-acid transaminase from Mycobacterium tuberculosis (MtIlvE) has been crystallized and its structure has been solved at 1.9 angstrom resolution. The MtIlvE monomer is composed of two domains that interact to form the active site. The biologically active form of IlvE is a homodimer in which each monomer contributes a substrate-specificity loop to the partner molecule. Additional substrate selectivity may be imparted by a conserved N-terminal Phe30 residue, which has previously been observed to shield the active site in the type IV fold homodimer. The active site of MtIlvE contains density corresponding to bound PMP, which is likely to be a consequence of the presence of tryptone in the crystallization medium. Additionally, two cysteine residues are positioned at the dimer interface for disulfide-bond formation under oxidative conditions. It is unknown whether they are involved in any regulatory activities analogous to those of the human mitochondrial branched-chain amino-acid transaminase. | ||
| - | + | The 1.9 A structure of the branched-chain amino-acid transaminase (IlvE) from Mycobacterium tuberculosis.,Tremblay LW, Blanchard JS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1071-7. Epub 2009 Oct 13. PMID:19923721<ref>PMID:19923721</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3ht5" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycobacterium tuberculosis]] | ||
| + | [[Category: Blanchard JS]] | ||
| + | [[Category: Tremblay LW]] | ||
Current revision
Crystal Structure of IlvE a Branched Chain Amino Acid Transaminase from Mycobacterium tuberculosis
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