View source for 7cbb


==Crystal structure of SbnC in the biosynthesis of staphyloferrin B==
<StructureSection load='7cbb' size='340' side='right'caption='[[7cbb]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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='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>
</table>
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== 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<ref>PMID:32880431</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Ju Y]]
[[Category: Tang J]]
[[Category: Zhou H]]