4w5k: Difference between revisions
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<StructureSection load='4w5k' size='340' side='right'caption='[[4w5k]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='4w5k' size='340' side='right'caption='[[4w5k]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4w5k]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W5K OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4w5k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei_TREU927 Trypanosoma brucei brucei TREU927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W5K FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=4w5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w5k OCA], [https://pdbe.org/4w5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w5k RCSB], [https://www.ebi.ac.uk/pdbsum/4w5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w5k 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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Trypanosoma brucei brucei TREU927]] | |||
[[Category: Trypanosoma brucei]] | |||
Latest revision as of 10:28, 27 September 2023
Structure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei, K237A mutantStructure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei, K237A mutant
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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