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5t8u

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Current revision (12:56, 4 October 2023) (edit) (undo)
 
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<StructureSection load='5t8u' size='340' side='right'caption='[[5t8u]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
<StructureSection load='5t8u' size='340' side='right'caption='[[5t8u]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5t8u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T8U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5t8u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T8U FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LPA:LIPOIC+ACID'>LPA</scene></td></tr>
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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]] 2.324&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF3D7_1314600 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</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=LPA:LIPOIC+ACID'>LPA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.63 2.7.7.63] </span></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=5t8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t8u OCA], [https://pdbe.org/5t8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t8u RCSB], [https://www.ebi.ac.uk/pdbsum/5t8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t8u ProSAT]</span></td></tr>
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<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=5t8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t8u OCA], [http://pdbe.org/5t8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t8u RCSB], [http://www.ebi.ac.uk/pdbsum/5t8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t8u ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIPLA_PLAF7 LIPLA_PLAF7] Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes (PubMed:17244193, PubMed:25116855, PubMed:28543853). In the mitochondrion, functions as a redox switch between two lipoylation routes (PubMed:25116855). Senses the oxidation state of lipoate and determines which downstream enzymes will be lipoylated (PubMed:25116855). In low reducing conditions, uses lipoate in its oxidized ring form to lipoylate glycine cleavage system H-protein GCVH (PubMed:17244193, PubMed:25116855, PubMed:28543853). In high reducing conditions and together with LipL2, uses reduced lipoate (dihydrolipoate) to lipoylate the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha-ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction (PubMed:17244193, PubMed:25116855).<ref>PMID:17244193</ref> <ref>PMID:25116855</ref> <ref>PMID:28543853</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Plaf7]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Transferase]]
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[[Category: Afanador GA]]
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[[Category: Afanador, G A]]
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[[Category: Guerra AJ]]
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[[Category: Guerra, A J]]
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[[Category: Prigge ST]]
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[[Category: Prigge, S T]]
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[[Category: Ligase]]
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[[Category: Lipoylation]]
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Current revision

Crystal structure of P. falciparum LipL1 in complex lipoate

PDB ID 5t8u

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