4eu1: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Structure of a mitochondrial aspartate aminotransferase from Trypanosoma brucei==
-<StructureSection load='4eu1' size='340' side='right' caption='[[4eu1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='4eu1' size='340' side='right'caption='[[4eu1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4eu1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trypanosoma_(trypanozoon)_brucei Trypanosoma (trypanozoon) 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EU1 FirstGlance]. <br>
+<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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tb11.02.2740 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5691 Trypanosoma (Trypanozoon) brucei])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=4eu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eu1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eu1 RCSB], [http://www.ebi.ac.uk/pdbsum/4eu1 PDBsum]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q385Q9_TRYB2 Q385Q9_TRYB2]
-The 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<ref>PMID:25945710</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Aspartate Aminotransferase|Aspartate Aminotransferase]]
+*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Aspartate transaminase]]
+[[Category: Large Structures]]
-[[Category: Structural genomic]]
+[[Category: Trypanosoma brucei]]
-[[Category: Aspartate aminotransferase]]
-[[Category: Mitochondrial]]
-[[Category: Pyridoxalphosphate lysine]]
-[[Category: Ssgcid]]
-[[Category: Transferase]]