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| | ==Crystal Structure of HbpS with bound iron== | | ==Crystal Structure of HbpS with bound iron== |
| - | <StructureSection load='3fpw' size='340' side='right' caption='[[3fpw]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3fpw' size='340' side='right'caption='[[3fpw]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fpw]] is a 1 chain structure with sequence from [http://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=3FPW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FPW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fpw]] 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=3FPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FPW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fpv|3fpv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hbpS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1926 "Streptomyces reticuli" (Waksman and Curtis) Waksman and Henrici])</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=3fpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpw OCA], [https://pdbe.org/3fpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fpw RCSB], [https://www.ebi.ac.uk/pdbsum/3fpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpw ProSAT]</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=3fpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpw OCA], [http://pdbe.org/3fpw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fpw RCSB], [http://www.ebi.ac.uk/pdbsum/3fpw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9RIM2_STRRE Q9RIM2_STRRE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/3fpw_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/3fpw_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bogel, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Groves, M R]] | + | [[Category: Streptomyces reticuli]] |
| - | [[Category: Lucana, D Ortiz de Orue]] | + | [[Category: Bogel G]] |
| - | [[Category: Zou, P]] | + | [[Category: Groves MR]] |
| - | [[Category: Haem binding]] | + | [[Category: Ortiz de Orue Lucana D]] |
| - | [[Category: Heme binding protein]] | + | [[Category: Zou P]] |
| Structural highlights
Function
Q9RIM2_STRRE
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
HbpS, a novel protein of previously unknown function from Streptomyces reticuli, is up-regulated in response to haemin- and peroxide-based oxidative stress and interacts with the SenS/SenR two-component signal transduction system. In this study, we report the high-resolution crystal structures (2.2 and 1.6 A) of octomeric HbpS crystallized in the presence and in the absence of haem and demonstrate that iron binds to surface-exposed lysine residues of an octomeric assembly. Based on an analysis of the crystal structures, we propose that the iron atom originates from the haem group and report subsequent biochemical experiments that demonstrate that HbpS possesses haem-degrading activity in vitro. Further examination of the crystal structures has identified amino acids that are essential for assembly of the octomer. The role of these residues is confirmed by biophysical experiments. Additionally, we show that while the octomeric assembly state of HbpS is not essential for haem-degrading activity, the assembly of HbpS is required for its interaction with the cognate sensor kinase, SenS. Homologs of HbpS and SenS/SenR have been identified in a number of medically and ecologically relevant bacterial species (including Vibrio cholerae, Klebsiella pneumoniae, Corynebacterium diphtheriae, Arthrobacter aurescens and Pseudomonas putida), suggesting the existence of a previously undescribed bacterial oxidative stress-response pathway common to Gram-negative and Gram-positive bacteria. Thus, the data presented provide the first insight into the function of a novel protein family and an example of an iron-mediated interaction between an accessory protein and its cognate two-component sensor kinase.
The oligomeric assembly of the novel haem-degrading protein HbpS is essential for interaction with its cognate two-component sensor kinase.,Lucana DO, Bogel G, Zou P, Groves MR J Mol Biol. 2009 Mar 6;386(4):1108-22. PMID:19244623[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lucana DO, Bogel G, Zou P, Groves MR. The oligomeric assembly of the novel haem-degrading protein HbpS is essential for interaction with its cognate two-component sensor kinase. J Mol Biol. 2009 Mar 6;386(4):1108-22. PMID:19244623
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