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3gfv

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Revision as of 21:29, 25 December 2014

Crystal Structure of Petrobactin-binding Protein YclQ from Bacillu subtilis

Structural highlights

3gfv is a 2 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Gene:	BSU03830, yclQ (Bacillus subtilis subsp. subtilis str. 168)
Resources:	FirstGlance, OCA, RCSB, PDBsum, TOPSAN

Function

[YCLQ_BACSU] Probably part of an ABC transporter complex.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Iron deprivation activates the expression of components of the siderophore-mediated iron acquisition systems in Bacillus subtilis, including not only the synthesis and uptake of its siderophore bacillibactin but also expression of multiple ABC transporters for iron scavenging using xenosiderophores. The yclNOPQ operon is shown to encode the complete transporter for petrobactin (PB), a photoreactive 3,4-catecholate siderophore produced by many members of the B. cereus group, including B. anthracis. Isogenic disruption mutants in the yclNOPQ transporter, including permease YclN, ATPase YclP, and a substrate-binding protein YclQ, are unable to use either PB or the photoproduct of FePB (FePB(nu)) for iron delivery and growth, in contrast to the wild-type B. subtilis. Complementation of the mutations with the copies of the respective genes restores this capability. The YclQ receptor binds selectively iron-free and ferric PB, the PB precursor, 3,4-dihydroxybenzoic acid (3,4-DHB), and FePB(nu) with high affinity; the ferric complexes are seen in ESI-MS, implying strong electrostatic interaction between the protein-binding pocket and siderophore. The first structure of a gram-positive siderophore receptor is presented. The 1.75-A crystal structure of YclQ reveals a bilobal periplasmic binding protein (PBP) fold consisting of two alpha/beta/alpha sandwich domains connected by a long alpha-helix with the binding pocket containing conserved positively charged and aromatic residues and large enough to accommodate FePB. Orthologs of the B. subtilis PB-transporter YclNOPQ in PB-producing Bacilli are likely contributors to the pathogenicity of these species and provide a potential target for antibacterial strategies.

Characterization of a Bacillus subtilis transporter for petrobactin, an anthrax stealth siderophore.,Zawadzka AM, Kim Y, Maltseva N, Nichiporuk R, Fan Y, Joachimiak A, Raymond KN Proc Natl Acad Sci U S A. 2009 Dec 22;106(51):21854-9. Epub 2009 Dec 2. PMID:19955416^[1]

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

References

↑ Zawadzka AM, Kim Y, Maltseva N, Nichiporuk R, Fan Y, Joachimiak A, Raymond KN. Characterization of a Bacillus subtilis transporter for petrobactin, an anthrax stealth siderophore. Proc Natl Acad Sci U S A. 2009 Dec 22;106(51):21854-9. Epub 2009 Dec 2. PMID:19955416

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3gfv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GFV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GFV FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr><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='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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU03830, yclQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 Bacillus subtilis subsp. subtilis str. 168])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU03830, yclQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 Bacillus subtilis subsp. subtilis str. 168])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gfv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gfv RCSB], [http://www.ebi.ac.uk/pdbsum/3gfv PDBsum], [http://www.topsan.org/Proteins/MCSG/3gfv TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gfv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gfv RCSB], [http://www.ebi.ac.uk/pdbsum/3gfv PDBsum], [http://www.topsan.org/Proteins/MCSG/3gfv TOPSAN]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/YCLQ_BACSU YCLQ_BACSU]] Probably part of an ABC transporter complex.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 </StructureSection>
 [[Category: Bacillus subtilis subsp. subtilis str. 168]]
-[[Category: Joachimiak, A.]]
+[[Category: Joachimiak, A]]
-[[Category: Kim, Y.]]
+[[Category: Kim, Y]]
-[[Category: MCSG, Midwest Center for Structural Genomics.]]
+[[Category: Structural genomic]]
-[[Category: Maltseva, N.]]
+[[Category: Maltseva, N]]
-[[Category: Raymond, K N.]]
+[[Category: Raymond, K N]]
-[[Category: Zawadzka, A M.]]
+[[Category: Zawadzka, A M]]
 [[Category: Alpha-beta-sandwich]]
 [[Category: Mcsg]]
-[[Category: Midwest center for structural genomic]]
+[[Category: PSI, Protein structure initiative]]
-[[Category: Protein structure initiative]]
-[[Category: Psi-2]]
 [[Category: Secreted]]
-[[Category: Structural genomic]]
 [[Category: Transport]]
 [[Category: Transport protein]]
 [[Category: Unknown function]]

3gfv

From Proteopedia

Revision as of 21:29, 25 December 2014

Crystal Structure of Petrobactin-binding Protein YclQ from Bacillu subtilis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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