|
|
| Line 3: |
Line 3: |
| | <StructureSection load='7cbb' size='340' side='right'caption='[[7cbb]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='7cbb' size='340' side='right'caption='[[7cbb]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7cbb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CBB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7CBB FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CBB FirstGlance]. <br> |
| - | </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></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]] 2.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sbnC, DDL17_05250, M1K003_0650 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=7cbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cbb OCA], [https://pdbe.org/7cbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cbb RCSB], [https://www.ebi.ac.uk/pdbsum/7cbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cbb 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=7cbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cbb OCA], [http://pdbe.org/7cbb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7cbb RCSB], [http://www.ebi.ac.uk/pdbsum/7cbb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7cbb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 23: |
Line 22: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ju, Y]] | + | [[Category: Ju Y]] |
| - | [[Category: Tang, J]] | + | [[Category: Tang J]] |
| - | [[Category: Zhou, H]] | + | [[Category: Zhou H]] |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Cupped hand fold]]
| + | |
| - | [[Category: Siderophore synthetase]]
| + | |
| - | [[Category: Type b nis synthetase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Staphyloferrin B is a key siderophore secreted by Staphylococcus aureus to acquire ferric ions from a host during infection, and its biosynthetic pathway has been validated to develop efficient antibacterial agents. Herein, we report the crystal structure of AMP-bound SbnC from S. aureus (SaSbnC) as the first representative structure of type B synthetases in the biosynthesis of alpha-hydroxycarboxylate siderophores. While type B synthetases specifically use alpha-ketoglutarate (alpha-KG) as their carboxylic acid substrate, SaSbnC showed unique structural features in the substrate pocket compared with the type A and C synthetases. Screening of alpha-KG analogues suggested that the hydrogen-bonding interaction between the alpha-carbonyl group of alpha-KG and residue Lys552 is a key determinant for the substrate selectivity of type B synthetases. Interestingly, citrate, the product of the tricarboxylic acid cycle and the substrate of type A synthetases, was found to inhibit the activity of SaSbnC with an IC50 value of 83 muM by mimicking alpha-KG binding, suggesting a potential regulatory role of the tricarboxylic acid cycle, whose activity is under the control of the intracellular iron concentration, to SaSbnC and other type B synthetases. These results provide critical new information to understand the structure, function, and regulation of type B synthetases in the siderophore-based iron acquisition system employed by a large number of pathogenic microbes.
Structural and Biochemical Characterization of SbnC as a Representative Type B Siderophore Synthetase.,Tang J, Ju Y, Zhou J, Guo J, Gu Q, Xu J, Zhou H ACS Chem Biol. 2020 Sep 18. doi: 10.1021/acschembio.0c00523. PMID:32880431[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang J, Ju Y, Zhou J, Guo J, Gu Q, Xu J, Zhou H. Structural and Biochemical Characterization of SbnC as a Representative Type B Siderophore Synthetase. ACS Chem Biol. 2020 Sep 18. doi: 10.1021/acschembio.0c00523. PMID:32880431 doi:http://dx.doi.org/10.1021/acschembio.0c00523
|
