4h51

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==Crystal structure of a putative Aspartate Aminotransferase from Leishmania major Friedlin==
==Crystal structure of a putative Aspartate Aminotransferase from Leishmania major Friedlin==
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<StructureSection load='4h51' size='340' side='right' caption='[[4h51]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='4h51' size='340' side='right'caption='[[4h51]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4h51]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_major_mhom/il/81/friedlin Leishmania major mhom/il/81/friedlin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H51 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H51 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4h51]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major_strain_Friedlin Leishmania major strain Friedlin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H51 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr><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>
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<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=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asat, LMJF_24_0370, LMJF_35_0820 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=347515 Leishmania major MHOM/IL/81/Friedlin])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4h51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h51 OCA], [https://pdbe.org/4h51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h51 RCSB], [https://www.ebi.ac.uk/pdbsum/4h51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h51 ProSAT]</span></td></tr>
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<tr><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>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4h51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h51 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h51 RCSB], [http://www.ebi.ac.uk/pdbsum/4h51 PDBsum]</span></td></tr>
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== Function ==
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<table>
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[https://www.uniprot.org/uniprot/Q4FX34_LEIMA Q4FX34_LEIMA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4h51" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aspartate transaminase]]
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[[Category: Large Structures]]
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[[Category: Leishmania major mhom/il/81/friedlin]]
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[[Category: Leishmania major strain Friedlin]]
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[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]
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[[Category: Aspartate aminotransferase]]
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[[Category: Leishmania major]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Seattle structural genomics center for infectious disease]]
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[[Category: Ssgcid]]
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[[Category: Structural genomic]]
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[[Category: Transferase]]
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Current revision

Crystal structure of a putative Aspartate Aminotransferase from Leishmania major Friedlin

PDB ID 4h51

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