4ix8: Difference between revisions
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==Crystal structure of Tyrosine aminotransferase from Leishmania infantum== | |||
<StructureSection load='4ix8' size='340' side='right'caption='[[4ix8]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ix8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_infantum Leishmania infantum]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4IX8 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]] 2.35Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ix8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ix8 OCA], [https://pdbe.org/4ix8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ix8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ix8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ix8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A4IDL0_LEIIN A4IDL0_LEIIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:24817714</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ix8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Leishmania infantum]] | |||
Latest revision as of 18:32, 20 September 2023
Crystal structure of Tyrosine aminotransferase from Leishmania infantumCrystal structure of Tyrosine aminotransferase from Leishmania infantum
Structural highlights
FunctionPublication 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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