6p63
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6p63 is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Wild-type NIS synthetase DesD bound to AMP and substrate analog cadaverine== | |
| + | <StructureSection load='6p63' size='340' side='right'caption='[[6p63]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6p63]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P63 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6p63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p63 OCA], [https://pdbe.org/6p63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p63 RCSB], [https://www.ebi.ac.uk/pdbsum/6p63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p63 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9L069_STRCO Q9L069_STRCO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The understudied nonribosomal-peptide-synthetase-independent siderophore (NIS) synthetase family has been increasingly associated with virulence in bacterial species due to its key role in the synthesis of hydroxamate and carboxylate "stealth" siderophores. We have identified a model family member, DesD, from Streptomyces coelicolor, to structurally characterize using a combination of a wild-type and a Arg306Gln variant in apo, cofactor product AMP-bound, and cofactor reactant ATP-bound complexes. The kinetics in the family has been limited by solubility and reporter assays, so we have developed a label-free kinetics assay utilizing a single-injection isothermal-titration-calorimetry-based method. We report second-order rate constants that are 50 times higher than the previous estimations for DesD. Our Arg306Gln DesD variant was also tested under identical buffer and substrate conditions, and its undetectable activity was confirmed. These are the first reported structures for DesD, and they describe the critical cofactor coordination. This is also the first label-free assay to unambiguously determine the kinetics for an NIS synthetase. | ||
| - | + | Cofactor Complexes of DesD, a Model Enzyme in the Virulence-related NIS Synthetase Family.,Hoffmann KM, Goncuian ES, Karimi KL, Amendola CR, Mojab Y, Wood KM, Prussia GA, Nix J, Yamamoto M, Lathan K, Orion IW Biochemistry. 2020 Sep 22;59(37):3427-3437. doi: 10.1021/acs.biochem.9b00899., Epub 2020 Sep 4. PMID:32885650<ref>PMID:32885650</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6p63" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces coelicolor]] | ||
| + | [[Category: Hoffmann KM]] | ||
Current revision
Wild-type NIS synthetase DesD bound to AMP and substrate analog cadaverine
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