3to3

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of Petrobactin Biosynthesis Protein AsbB from Bacillus anthracis str. Sterne

Structural highlights

3to3 is a 2 chain structure with sequence from Bacillus anthracis str. Sterne. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.382Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASBB_BACAN Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence (PubMed:16875672, PubMed:17189355, PubMed:22408253). Catalyzes the ATP-dependent condensation of spermidine with N(8)-citryl-spermidine or N(1)-(3,4-dihydroxbenzoyl)-N(8)-citryl-spermidine, two intermediates in petrobactin biosynthesis pathway (PubMed:18758617, PubMed:22408253).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Petrobactin, a mixed catechol-carboxylate siderophore, is required for full virulence of Bacillus anthracis, the causative agent of anthrax. The asbABCDEF operon encodes the biosynthetic machinery for this secondary metabolite. Here, we show that the function of five gene products encoded by the asb operon is necessary and sufficient for conversion of endogenous precursors to petrobactin using an in vitro system. In this pathway, the siderophore synthetase AsbB catalyzes formation of amide bonds crucial for petrobactin assembly through use of biosynthetic intermediates, as opposed to primary metabolites, as carboxylate donors. In solving the crystal structure of the B. anthracis siderophore biosynthesis protein B (AsbB), we disclose a three-dimensional model of a nonribosomal peptide synthetase-independent siderophore (NIS) synthetase. Structural characteristics provide new insight into how this bifunctional condensing enzyme can bind and adenylate multiple citrate-containing substrates followed by incorporation of both natural and unnatural polyamine nucleophiles. This activity enables formation of multiple end-stage products leading to final assembly of petrobactin. Subsequent enzymatic assays with the nonribosomal peptide synthetase-like AsbC, AsbD, and AsbE polypeptides show that the alternative products of AsbB are further converted to petrobactin, verifying previously proposed convergent routes to formation of this siderophore. These studies identify potential therapeutic targets to halt deadly infections caused by B. anthracis and other pathogenic bacteria and suggest new avenues for the chemoenzymatic synthesis of novel compounds.

Functional and Structural Analysis of the Siderophore Synthetase AsbB through Reconstitution of the Petrobactin Biosynthetic Pathway from Bacillus anthracis.,Nusca TD, Kim Y, Maltseva N, Lee JY, Eschenfeldt W, Stols L, Schofield MM, Scaglione JB, Dixon SD, Oves-Costales D, Challis GL, Hanna PC, Pfleger BF, Joachimiak A, Sherman DH J Biol Chem. 2012 May 4;287(19):16058-72. Epub 2012 Mar 9. PMID:22408253^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wilson MK, Abergel RJ, Raymond KN, Arceneaux JE, Byers BR. Siderophores of Bacillus anthracis, Bacillus cereus, and Bacillus thuringiensis. Biochem Biophys Res Commun. 2006 Sep 15;348(1):320-5. PMID:16875672 doi:10.1016/j.bbrc.2006.07.055
↑ Lee JY, Janes BK, Passalacqua KD, Pfleger BF, Bergman NH, Liu H, Håkansson K, Somu RV, Aldrich CC, Cendrowski S, Hanna PC, Sherman DH. Biosynthetic analysis of the petrobactin siderophore pathway from Bacillus anthracis. J Bacteriol. 2007 Mar;189(5):1698-710. PMID:17189355 doi:10.1128/JB.01526-06
↑ Oves-Costales D, Kadi N, Fogg MJ, Song L, Wilson KS, Challis GL. Petrobactin biosynthesis: AsbB catalyzes condensation of spermidine with N8-citryl-spermidine and its N1-(3,4-dihydroxybenzoyl) derivative. Chem Commun (Camb). 2008 Sep 14;(34):4034-6. PMID:18758617 doi:10.1039/b809353a
↑ Nusca TD, Kim Y, Maltseva N, Lee JY, Eschenfeldt W, Stols L, Schofield MM, Scaglione JB, Dixon SD, Oves-Costales D, Challis GL, Hanna PC, Pfleger BF, Joachimiak A, Sherman DH. Functional and Structural Analysis of the Siderophore Synthetase AsbB through Reconstitution of the Petrobactin Biosynthetic Pathway from Bacillus anthracis. J Biol Chem. 2012 May 4;287(19):16058-72. Epub 2012 Mar 9. PMID:22408253 doi:10.1074/jbc.M112.359349
↑ Nusca TD, Kim Y, Maltseva N, Lee JY, Eschenfeldt W, Stols L, Schofield MM, Scaglione JB, Dixon SD, Oves-Costales D, Challis GL, Hanna PC, Pfleger BF, Joachimiak A, Sherman DH. Functional and Structural Analysis of the Siderophore Synthetase AsbB through Reconstitution of the Petrobactin Biosynthetic Pathway from Bacillus anthracis. J Biol Chem. 2012 May 4;287(19):16058-72. Epub 2012 Mar 9. PMID:22408253 doi:10.1074/jbc.M112.359349

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3to3"

@@ Line 3: / Line 3: @@
 <StructureSection load='3to3' size='340' side='right'caption='[[3to3]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3to3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_(strain_sterne) Bacillus anthracis (strain sterne)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TO3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3to3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Sterne Bacillus anthracis str. Sterne]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TO3 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.382&#8491;</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asbB, BA_1982, GBAA_1982 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=260799 Bacillus anthracis (strain Sterne)])</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=3to3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to3 OCA], [https://pdbe.org/3to3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3to3 RCSB], [https://www.ebi.ac.uk/pdbsum/3to3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3to3 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ASBB_BACAN ASBB_BACAN] Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence (PubMed:16875672, PubMed:17189355, PubMed:22408253). Catalyzes the ATP-dependent condensation of spermidine with N(8)-citryl-spermidine or N(1)-(3,4-dihydroxbenzoyl)-N(8)-citryl-spermidine, two intermediates in petrobactin biosynthesis pathway (PubMed:18758617, PubMed:22408253).<ref>PMID:16875672</ref> <ref>PMID:17189355</ref> <ref>PMID:18758617</ref> <ref>PMID:22408253</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Bacillus anthracis str. Sterne]]
 [[Category: Large Structures]]
-[[Category: Eschenfeldt, W]]
+[[Category: Eschenfeldt W]]
-[[Category: Joachimiak, A]]
+[[Category: Joachimiak A]]
-[[Category: Kim, Y]]
+[[Category: Kim Y]]
-[[Category: Structural genomic]]
+[[Category: Stols L]]
-[[Category: Stols, L]]
-[[Category: Adenylation]]
-[[Category: Alpha-beta structure]]
-[[Category: Biosynthetic protein]]
-[[Category: Cytosol]]
-[[Category: Mcsg]]
-[[Category: Psi-biology]]

3to3

From Proteopedia

Current revision

Crystal Structure of Petrobactin Biosynthesis Protein AsbB from Bacillus anthracis str. Sterne

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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