4eu1: Difference between revisions
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==Structure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei== | ==Structure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei== | ||
<StructureSection load='4eu1' size='340' side='right' caption='[[4eu1]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4eu1' size='340' side='right'caption='[[4eu1]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4eu1]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4eu1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EU1 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>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | </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=EDO:1,2-ETHANEDIOL'>EDO</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=4eu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eu1 OCA], [https://pdbe.org/4eu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eu1 RCSB], [https://www.ebi.ac.uk/pdbsum/4eu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eu1 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q385Q9_TRYB2 Q385Q9_TRYB2] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Aspartate | *[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Trypanosoma brucei]] | ||
Revision as of 07:16, 7 October 2022
Structure of a mitochondrial aspartate aminotransferase from Trypanosoma bruceiStructure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei
Structural highlights
FunctionPublication Abstract from PubMedThe structures of three aspartate aminotransferases (AATs) from eukaryotic pathogens were solved within the Seattle Structural Genomics Center for Infectious Disease (SSGCID). Both the open and closed conformations of AAT were observed. Pyridoxal phosphate was bound to the active site via a Schiff base to a conserved lysine. An active-site mutant showed that Trypanosoma brucei AAT still binds pyridoxal phosphate even in the absence of the tethering lysine. The structures highlight the challenges for the structure-based design of inhibitors targeting the active site, while showing options for inhibitor design targeting the N-terminal arm. Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.,Abendroth J, Choi R, Wall A, Clifton MC, Lukacs CM, Staker BL, Van Voorhis W, Myler P, Lorimer DD, Edwards TE Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):566-71. doi:, 10.1107/S2053230X15001831. Epub 2015 Apr 21. PMID:25945710[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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