6om5
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Structure of a haemophore from Haemophilus haemolyticus== | |
+ | <StructureSection load='6om5' size='340' side='right'caption='[[6om5]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6om5]] is a 1 chain structure. 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> | ||
+ | </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> | ||
+ | <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> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6om5" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Gell, D A]] | ||
+ | [[Category: Guss, J M]] | ||
+ | [[Category: Mackay, J P]] | ||
[[Category: Torrado, M]] | [[Category: Torrado, M]] | ||
- | [[Category: Walshe, J | + | [[Category: Walshe, J L]] |
- | [[Category: | + | [[Category: Antimicrobial]] |
- | [[Category: | + | [[Category: Haemophilus haemolyticus]] |
- | [[Category: | + | [[Category: Haemophore]] |
+ | [[Category: Metal transport]] |
Revision as of 08:12, 4 December 2019
Structure of a haemophore from Haemophilus haemolyticus
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