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New page: '''Unreleased structure''' The entry 3os6 is ON HOLD Authors: Domagalski, M.J., Chruszcz, M., Skarina, T., Onopriyenko, O., Cymborowski, M., Savchenko, A., Edwards, A., Anderson, W., Mi... |
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The | ==Crystal structure of putative 2,3-dihydroxybenzoate-specific isochorismate synthase, DhbC from Bacillus anthracis.== | ||
<StructureSection load='3os6' size='340' side='right'caption='[[3os6]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3os6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Ames Bacillus anthracis str. Ames]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OS6 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=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3os6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3os6 OCA], [https://pdbe.org/3os6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3os6 RCSB], [https://www.ebi.ac.uk/pdbsum/3os6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3os6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A6H3A7J7_BACAN A0A6H3A7J7_BACAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The isochorismate synthase DhbC from Bacillus anthracis is essential for the biosynthesis of the siderophore bacillibactin by this pathogenic bacterium. The structure of the selenomethionine-substituted protein was determined to 2.4 A resolution using single-wavelength anomalous diffraction. B. anthracis DhbC bears the strongest resemblance to the Escherichia coli isochorismate synthase EntC, which is involved in the biosynthesis of another siderophore, namely enterobactin. Both proteins adopt the characteristic fold of other chorismate-utilizing enzymes, which are involved in the biosynthesis of various products, including siderophores, menaquinone and tryptophan. The conservation of the active-site residues, as well as their spatial arrangement, suggests that these enzymes share a common Mg(2+)-dependent catalytic mechanism. | |||
Structure of isochorismate synthase DhbC from Bacillus anthracis.,Domagalski MJ, Tkaczuk KL, Chruszcz M, Skarina T, Onopriyenko O, Cymborowski M, Grabowski M, Savchenko A, Minor W Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):956-61. doi: , 10.1107/S1744309113021246. Epub 2013 Aug 19. PMID:23989140<ref>PMID:23989140</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3os6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus anthracis str. Ames]] | |||
[[Category: Large Structures]] | |||
[[Category: Anderson W]] | |||
[[Category: Chruszcz M]] | |||
[[Category: Cymborowski M]] | |||
[[Category: Domagalski MJ]] | |||
[[Category: Edwards A]] | |||
[[Category: Minor W]] | |||
[[Category: Onopriyenko O]] | |||
[[Category: Savchenko A]] | |||
[[Category: Skarina T]] | |||
Latest revision as of 15:46, 17 January 2024
Crystal structure of putative 2,3-dihydroxybenzoate-specific isochorismate synthase, DhbC from Bacillus anthracis.Crystal structure of putative 2,3-dihydroxybenzoate-specific isochorismate synthase, DhbC from Bacillus anthracis.
Structural highlights
FunctionPublication Abstract from PubMedThe isochorismate synthase DhbC from Bacillus anthracis is essential for the biosynthesis of the siderophore bacillibactin by this pathogenic bacterium. The structure of the selenomethionine-substituted protein was determined to 2.4 A resolution using single-wavelength anomalous diffraction. B. anthracis DhbC bears the strongest resemblance to the Escherichia coli isochorismate synthase EntC, which is involved in the biosynthesis of another siderophore, namely enterobactin. Both proteins adopt the characteristic fold of other chorismate-utilizing enzymes, which are involved in the biosynthesis of various products, including siderophores, menaquinone and tryptophan. The conservation of the active-site residues, as well as their spatial arrangement, suggests that these enzymes share a common Mg(2+)-dependent catalytic mechanism. Structure of isochorismate synthase DhbC from Bacillus anthracis.,Domagalski MJ, Tkaczuk KL, Chruszcz M, Skarina T, Onopriyenko O, Cymborowski M, Grabowski M, Savchenko A, Minor W Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):956-61. doi: , 10.1107/S1744309113021246. Epub 2013 Aug 19. PMID:23989140[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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