5udt: Difference between revisions
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<StructureSection load='5udt' size='340' side='right' caption='[[5udt]], [[Resolution|resolution]] 3.19Å' scene=''> | <StructureSection load='5udt' size='340' side='right' caption='[[5udt]], [[Resolution|resolution]] 3.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5udt]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UDT FirstGlance]. <br> | <table><tr><td colspan='2'>[[5udt]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacpl Lacpl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UDT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UDT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5udr|5udr]], [[5uds|5uds]], [[5udu|5udu]], [[5udv|5udv]], [[5udw|5udw]], [[5udx|5udx]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5udr|5udr]], [[5uds|5uds]], [[5udu|5udu]], [[5udv|5udv]], [[5udw|5udw]], [[5udx|5udx]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">larE, lp_0109 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=220668 LACPL])</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=5udt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5udt OCA], [http://pdbe.org/5udt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5udt RCSB], [http://www.ebi.ac.uk/pdbsum/5udt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5udt ProSAT]</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=5udt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5udt OCA], [http://pdbe.org/5udt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5udt RCSB], [http://www.ebi.ac.uk/pdbsum/5udt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5udt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Lacpl]] | |||
[[Category: Desguin, B]] | [[Category: Desguin, B]] | ||
[[Category: Fellner, M]] | [[Category: Fellner, M]] | ||
Revision as of 00:05, 16 November 2017
LarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with AMPLarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, in complex with AMP
Structural highlights
Publication Abstract from PubMedThe lar operon in Lactobacillus plantarum encodes five Lar proteins (LarA/B/C/D/E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. Previous studies have established that two molecules of LarE catalyze successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. However, the catalytic mechanism of this very unusual sulfur-sacrificing reaction remains elusive. In this work, we present the crystal structures of LarE in ligand-free and several ligand-bound forms, demonstrating that LarE is a member of the N-type ATP pyrophosphatase (PPase) family with a conserved N-terminal ATP PPase domain and a unique C-terminal domain harboring the putative catalytic site. Structural analysis, combined with structure-guided mutagenesis, leads us to propose a catalytic mechanism that establishes LarE as a paradigm for sulfur transfer through sacrificing its catalytic cysteine residue. Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.,Fellner M, Desguin B, Hausinger RP, Hu J Proc Natl Acad Sci U S A. 2017 Aug 22;114(34):9074-9079. doi:, 10.1073/pnas.1704967114. Epub 2017 Aug 7. PMID:28784764[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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