5t8u

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'''Unreleased structure'''
 
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The entry 5t8u is ON HOLD until Paper Publication
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==Crystal structure of P. falciparum LipL1 in complex lipoate==
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<StructureSection load='5t8u' size='340' side='right'caption='[[5t8u]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
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== Structural highlights ==
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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='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='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='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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</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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plasmodium falciparum lipoate protein ligase 1 (PfLipL1) is an ATP-dependent ligase that belongs to the biotin/lipoate A/B protein ligase family (PFAM PF03099). PfLipL1 is the only known canonical lipoate ligase in Pf and functions as a redox switch between two lipoylation routes in the parasite mitochondrion. Here, we report the crystal structure of a deletion construct of PfLipL1 (PfLipL1Delta243-279 ) bound to lipoate, and validate the lipoylation activity of this construct in both an in vitro lipoylation assay and a cell-based lipoylation assay. This characterization represents the first step in understanding the redox dependence of the lipoylation mechanism in malaria parasites. Proteins 2017. (c) 2017 Wiley Periodicals, Inc.
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Authors:
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Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.,Guerra AJ, Afanador GA, Prigge ST Proteins. 2017 May 24. doi: 10.1002/prot.25324. PMID:28543853<ref>PMID:28543853</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5t8u" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Afanador GA]]
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[[Category: Guerra AJ]]
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[[Category: Prigge ST]]

Current revision

Crystal structure of P. falciparum LipL1 in complex lipoate

PDB ID 5t8u

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