4ix8: Difference between revisions
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==Crystal structure of Tyrosine aminotransferase from Leishmania infantum== | ==Crystal structure of Tyrosine aminotransferase from Leishmania infantum== | ||
<StructureSection load='4ix8' size='340' side='right' caption='[[4ix8]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='4ix8' size='340' side='right' caption='[[4ix8]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
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<table><tr><td colspan='2'>[[4ix8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leiin Leiin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IX8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ix8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leiin Leiin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IX8 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LINJ_36_2490, TAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5671 LEIIN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LINJ_36_2490, TAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5671 LEIIN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine_transaminase Tyrosine transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.5 2.6.1.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine_transaminase Tyrosine transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.5 2.6.1.5] </span></td></tr> | ||
<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=4ix8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ix8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ix8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ix8 PDBsum]</span></td></tr> | <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=4ix8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ix8 OCA], [http://pdbe.org/4ix8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ix8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ix8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ix8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ix8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aminotransferase|Aminotransferase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:54, 11 August 2016
Crystal structure of Tyrosine aminotransferase from Leishmania infantumCrystal structure of Tyrosine aminotransferase from Leishmania infantum
Structural highlights
Publication Abstract from PubMedThe trypanosomatid parasite Leishmania infantum is the causative agent of visceral leishmaniasis (VL), which is usually fatal unless treated. VL has an incidence of 0.5 million cases every year and is an important opportunistic co-infection in HIV/AIDS. Tyrosine aminotransferase (TAT) has an important role in the metabolism of trypanosomatids, catalyzing the first step in the degradation pathway of aromatic amino acids, which are ultimately converted into their corresponding L-2-oxoacids. Unlike the enzyme in Trypanosoma cruzi and mammals, L. infantum TAT (LiTAT) is not able to transaminate ketoglutarate. Here, the structure of LiTAT at 2.35 A resolution is reported, and it is confirmed that the presence of two Leishmania-specific residues (Gln55 and Asn58) explains, at least in part, this specific reactivity. The difference in substrate specificity between leishmanial and mammalian TAT and the importance of this enzyme in parasite metabolism suggest that it may be a useful target in the development of new drugs against leishmaniasis. Structure of tyrosine aminotransferase from Leishmania infantum.,Moreno MA, Abramov A, Abendroth J, Alonso A, Zhang S, Alcolea PJ, Edwards T, Lorimer D, Myler PJ, Larraga V Acta Crystallogr F Struct Biol Commun. 2014 May;70(Pt 5):583-7. doi:, 10.1107/S2053230X14007845. Epub 2014 Apr 25. PMID:24817714[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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