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4bmw

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Crystal structure of the Streptomyces reticuli HbpS E78D, E81D double mutant

Structural highlights

4bmw is a 1 chain structure with sequence from Streptomyces reticuli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.99Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9RIM2_STRRE

Publication Abstract from PubMed

The soil bacterium Streptomyces reticuli secretes the octameric protein HbpS that acts as a sensory component of the redox-signalling pathway HbpS-SenS-SenR. This system modulates a genetic response on iron- and haem-mediated oxidative stress. Moreover, HbpS alone provides this bacterium with a defence mechanism to the presence of high concentrations of iron ions and haem. While the protection against haem has been related to its haem-binding and haem-degrading activity, the interaction with iron has not been studied in detail. In this work, we biochemically analyzed the iron-binding activity of a set of generated HbpS mutant proteins and present evidence showing the involvement of one internal and two exposed D/EXXE motifs in binding of high quantities of ferrous iron, with the internal E78XXE81 displaying the tightest binding. We additionally show that HbpS is able to oxidize ferrous to ferric iron ions. Based on the crystal structure of both the wild-type and the mutant HbpS-D78XXD81, we conclude that the local arrangement of the side chains from the glutamates in E78XXE81 within the octameric assembly is a pre-requisite for interaction with iron. The data obtained led us to propose that the exposed and the internal motif build a highly specific route that is involved in the transport of high quantities of iron ions into the core of the HbpS octamer. Furthermore, physiological studies using Streptomyces transformants secreting either wild-type or HbpS mutant proteins and different redox-cycling compounds led us to conclude that the iron-sequestering activity of HbpS protects these soil bacteria from the hazardous side effects of peroxide- and iron-based oxidative stress.

Iron Binding at Specific Sites within the Octameric HbpS Protects Streptomycetes from Iron-Mediated Oxidative Stress.,Wedderhoff I, Kursula I, Groves MR, Ortiz de Orue Lucana D PLoS One. 2013 Aug 27;8(8):e71579. doi: 10.1371/journal.pone.0071579. PMID:24013686^[1]

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

References

↑ Wedderhoff I, Kursula I, Groves MR, Ortiz de Orue Lucana D. Iron Binding at Specific Sites within the Octameric HbpS Protects Streptomycetes from Iron-Mediated Oxidative Stress. PLoS One. 2013 Aug 27;8(8):e71579. doi: 10.1371/journal.pone.0071579. PMID:24013686 doi:10.1371/journal.pone.0071579

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/4bmw"

@@ Line 3: / Line 3: @@
 <StructureSection load='4bmw' size='340' side='right'caption='[[4bmw]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4bmw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"streptomyces_reticuli"_(waksman_and_curtis)_waksman_and_henrici "streptomyces reticuli" (waksman and curtis) waksman and henrici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BMW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4bmw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_reticuli Streptomyces reticuli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BMW FirstGlance]. <br>
-</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=4bmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bmw OCA], [https://pdbe.org/4bmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bmw RCSB], [https://www.ebi.ac.uk/pdbsum/4bmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bmw ProSAT]</span></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]] 1.99&#8491;</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=4bmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bmw OCA], [https://pdbe.org/4bmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bmw RCSB], [https://www.ebi.ac.uk/pdbsum/4bmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bmw ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9RIM2_STRRE Q9RIM2_STRRE]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Groves, M R]]
+[[Category: Streptomyces reticuli]]
-[[Category: Kursula, I]]
+[[Category: Groves MR]]
-[[Category: Lucana, D Ortiz de Orue]]
+[[Category: Kursula I]]
-[[Category: Wagener, S]]
+[[Category: Ortiz de Orue Lucana D]]
-[[Category: Wedderhoff, I]]
+[[Category: Wagener S]]
-[[Category: Heme]]
+[[Category: Wedderhoff I]]
-[[Category: Iron binding]]
-[[Category: Metal binding protein]]
-[[Category: Oxidative stress]]

4bmw

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Current revision

Crystal structure of the Streptomyces reticuli HbpS E78D, E81D double mutant

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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