5t8u: Difference between revisions
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==Crystal structure of P. falciparum LipL1 in complex lipoate== | |||
<StructureSection load='5t8u' size='340' side='right' caption='[[5t8u]], [[Resolution|resolution]] 2.32Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5t8u]] is a 2 chain structure. 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> | |||
</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> | |||
<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> | |||
<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> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5t8u" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Transferase]] | |||
[[Category: Afanador, G A]] | |||
[[Category: Guerra, A J]] | |||
[[Category: Prigge, S T]] | |||
[[Category: Ligase]] | |||
[[Category: Lipoylation]] | |||
Revision as of 11:04, 3 August 2017
Crystal structure of P. falciparum LipL1 in complex lipoate
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