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| | <StructureSection load='3aeh' size='340' side='right'caption='[[3aeh]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3aeh' size='340' side='right'caption='[[3aeh]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3aeh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AEH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3aeh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AEH FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hbp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 2Å</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=3aeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeh OCA], [https://pdbe.org/3aeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aeh RCSB], [https://www.ebi.ac.uk/pdbsum/3aeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aeh ProSAT]</span></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=3aeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aeh OCA], [https://pdbe.org/3aeh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aeh RCSB], [https://www.ebi.ac.uk/pdbsum/3aeh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aeh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/HBP_ECOLX HBP_ECOLX]] Interacts with hemoglobin, degrades it and subsequently binds the released heme. Could make heme accessible not only for E.coli, but also for B.fragilis during mixed intra-abdominal infections. Has a role in abscess formation.<ref>PMID:9743528</ref> <ref>PMID:11748157</ref>
| + | [https://www.uniprot.org/uniprot/HBP_ECOLX HBP_ECOLX] Interacts with hemoglobin, degrades it and subsequently binds the released heme. Could make heme accessible not only for E.coli, but also for B.fragilis during mixed intra-abdominal infections. Has a role in abscess formation.<ref>PMID:9743528</ref> <ref>PMID:11748157</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Park, S Y]] | + | [[Category: Park S-Y]] |
| - | [[Category: Tajima, N]] | + | [[Category: Tajima N]] |
| - | [[Category: Tame, J R.H]] | + | [[Category: Tame JRH]] |
| - | [[Category: Auto-proteolytic]]
| + | |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Cell outer membrane]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Intein]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Reaction intermediate]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Virulence]]
| + | |
| Structural highlights
Function
HBP_ECOLX Interacts with hemoglobin, degrades it and subsequently binds the released heme. Could make heme accessible not only for E.coli, but also for B.fragilis during mixed intra-abdominal infections. Has a role in abscess formation.[1] [2]
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
Many virulence factors secreted by pathogenic Gram-negative bacteria are found to be members of the autotransporter protein family. These proteins share a common mechanism by which they exit the periplasm, involving the formation of a 12-stranded beta-barrel domain in the outer membrane. The role of this barrel in the secretion of the N-terminal passenger domain is controversial, and no model currently explains satisfactorily the entire body of experimental data. After secretion, some autotransporter barrels autoproteolytically cleave away the passenger, and one crystal structure is known for a barrel of this type in the postcleavage state. Hbp is an autotransporter of the self-cleaving type, which cuts the polypeptide between two absolutely conserved asparagine residues buried within the barrel lumen. Mutation of the first asparagine residue to isosteric aspartic acid prevents proteolysis. Here we present the crystal structure of a truncated Hbp mutant carrying the C-terminal residues of the passenger domain attached to the barrel. This model mimics the state of the protein immediately prior to separation of the passenger and barrel domains, and shows the role of residues in the so-called "linker" between the passenger and beta domains. This high-resolution membrane protein crystal structure also reveals the sites of many water molecules within the barrel. The cleavage mechanism shows similarities to those of inteins and some viral proteins, but with a novel means of promoting nucleophilic attack.
A novel intein-like autoproteolytic mechanism in autotransporter proteins.,Tajima N, Kawai F, Park SY, Tame JR J Mol Biol. 2010 Oct 1;402(4):645-56. Epub 2010 Jul 6. PMID:20615416[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Otto BR, van Dooren SJ, Nuijens JH, Luirink J, Oudega B. Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1. J Exp Med. 1998 Sep 21;188(6):1091-1103. PMID:9743528
- ↑ Otto BR, van Dooren SJ, Dozois CM, Luirink J, Oudega B. Escherichia coli hemoglobin protease autotransporter contributes to synergistic abscess formation and heme-dependent growth of Bacteroides fragilis. Infect Immun. 2002 Jan;70(1):5-10. PMID:11748157
- ↑ Tajima N, Kawai F, Park SY, Tame JR. A novel intein-like autoproteolytic mechanism in autotransporter proteins. J Mol Biol. 2010 Oct 1;402(4):645-56. Epub 2010 Jul 6. PMID:20615416 doi:http://dx.doi.org/10.1016/j.jmb.2010.06.068
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