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| <StructureSection load='6xrc' size='340' side='right'caption='[[6xrc]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='6xrc' size='340' side='right'caption='[[6xrc]], [[Resolution|resolution]] 2.45Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6xrc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XRC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XRC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6xrc]] is a 2 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=6XRC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XRC FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6nl2|6nl2]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCO2785 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 "Actinomyces coelicolor" (Muller 1908) Lieske 1921])</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=6xrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xrc OCA], [https://pdbe.org/6xrc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xrc RCSB], [https://www.ebi.ac.uk/pdbsum/6xrc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xrc ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xrc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xrc OCA], [http://pdbe.org/6xrc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xrc RCSB], [http://www.ebi.ac.uk/pdbsum/6xrc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xrc ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q9L069_STRCO Q9L069_STRCO] |
| <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]] |
- | [[Category: Hoffmann, K M]] | + | [[Category: Streptomyces coelicolor]] |
- | [[Category: Biosynthetic protein]] | + | [[Category: Hoffmann KM]] |
- | [[Category: Catalytic variant]]
| + | |
- | [[Category: Nis synthetase]]
| + | |
- | [[Category: Siderophore synthesis]]
| + | |
| Structural highlights
Function
Q9L069_STRCO
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hoffmann KM, Goncuian ES, Karimi KL, Amendola CR, Mojab Y, Wood KM, Prussia GA, Nix J, Yamamoto M, Lathan K, Orion IW. Cofactor Complexes of DesD, a Model Enzyme in the Virulence-related NIS Synthetase Family. Biochemistry. 2020 Sep 22;59(37):3427-3437. doi: 10.1021/acs.biochem.9b00899., Epub 2020 Sep 4. PMID:32885650 doi:http://dx.doi.org/10.1021/acs.biochem.9b00899
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