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6om5

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Current revision (14:52, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6om5' size='340' side='right'caption='[[6om5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='6om5' size='340' side='right'caption='[[6om5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6om5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_x"_pritchett_and_stillman_1919 "bacillus x" pritchett and stillman 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OM5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OM5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6om5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_haemolyticus Haemophilus haemolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OM5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<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=6om5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6om5 OCA], [http://pdbe.org/6om5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6om5 RCSB], [http://www.ebi.ac.uk/pdbsum/6om5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6om5 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6om5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6om5 OCA], [https://pdbe.org/6om5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6om5 RCSB], [https://www.ebi.ac.uk/pdbsum/6om5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6om5 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0M3G7Q5_HAEHA A0A0M3G7Q5_HAEHA]
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Commensal bacteria serve as an important line of defense against colonisation by opportunisitic pathogens, but the underlying molecular mechanisms remain poorly explored. Here, we show that strains of a commensal bacterium, Haemophilus haemolyticus, make hemophilin, a heme-binding protein that inhibits growth of the opportunistic pathogen, non-typeable Haemophilus influenzae (NTHi) in culture. We purified the NTHi-inhibitory protein from H. haemolyticus and identified the hemophilin gene using proteomics and a gene knockout. An x-ray crystal structure of recombinant hemophilin shows that the protein does not belong to any of the known heme-binding protein folds, suggesting that it evolved independently. Biochemical characterisation shows that heme can be captured in the ferrous or ferric state, and with a variety of small heme-ligands bound, suggesting that hemophilin could function under a range of physiological conditions. Hemophilin knockout bacteria show a limited capacity to utilise free heme for growth. Our data suggest that hemophilin is a hemophore and that inhibition of NTHi occurs by heme starvation, raising the possibility that competition from hemophilin-producing H. haemolyticus could antagonise NTHi colonisation in the respiratory tract.
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A heme-binding protein produced by Haemophilus haemolyticus inhibits non-typeable Haemophilus influenzae.,Latham RD, Torrado M, Atto B, Walshe JL, Wilson R, Guss JM, Mackay JP, Tristram S, Gell DA Mol Microbiol. 2019 Nov 19. doi: 10.1111/mmi.14426. PMID:31742788<ref>PMID:31742788</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6om5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus x pritchett and stillman 1919]]
 
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[[Category: Large Structures]]
 
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[[Category: Gell, D A]]
 
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[[Category: Guss, J M]]
 
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[[Category: Mackay, J P]]
 
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[[Category: Torrado, M]]
 
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[[Category: Walshe, J L]]
 
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[[Category: Antimicrobial]]
 
[[Category: Haemophilus haemolyticus]]
[[Category: Haemophilus haemolyticus]]
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[[Category: Haemophore]]
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[[Category: Large Structures]]
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[[Category: Metal transport]]
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[[Category: Gell DA]]
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[[Category: Guss JM]]
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[[Category: Mackay JP]]
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[[Category: Torrado M]]
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[[Category: Walshe JL]]

Current revision

Structure of a haemophore from Haemophilus haemolyticus

PDB ID 6om5

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