This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3ak5

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Hemoglobin protease (Hbp) passenger missing domain-2

Structural highlights

3ak5 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The autotransporter Tsh (temperature-sensitive haemagglutinin) secreted by avian pathogenic Escherichia coli was reported in 1994 and the almost identical Hbp (haemoglobin protease) was discovered some years later in isolates from patients suffering from peritoneal abscesses. However, the function of the protein remains uncertain. The crystal structure of Hbp shows that the protein carries a serine protease domain (domain 1) and a small domain of 75 residues called domain 2 which is inserted into the long beta-helix characteristic of autotransporter passenger proteins. In this paper, domain 1 is shown to bind calcium, although metal ions binding to this site do not seem to regulate protease activity. Tsh has been reported to bind red cells and components of the extracellular matrix, but it is demonstrated that these properties are not a consequence of the presence of domain 2.

Role of domains within the autotransporter Hbp/Tsh.,Nishimura K, Yoon YH, Kurihara A, Unzai S, Luirink J, Park SY, Tame JR Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1295-300. Epub, 2010 Nov 16. PMID:21123869^[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
↑ Nishimura K, Yoon YH, Kurihara A, Unzai S, Luirink J, Park SY, Tame JR. Role of domains within the autotransporter Hbp/Tsh. Acta Crystallogr D Biol Crystallogr. 2010 Dec;66(Pt 12):1295-300. Epub, 2010 Nov 16. PMID:21123869 doi:10.1107/S0907444910036966

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ak5"

Categories: Escherichia coli | Large Structures | Nishimura K | Park S-Y | Tame JRH

@@ Line 3: / Line 3: @@
 <StructureSection load='3ak5' size='340' side='right'caption='[[3ak5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ak5]] is a 4 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=3AK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AK5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ak5]] is a 4 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=3AK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AK5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wxr|1wxr]], [[3h09|3h09]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ak5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ak5 OCA], [https://pdbe.org/3ak5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ak5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ak5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ak5 ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Nishimura, K]]
+[[Category: Nishimura K]]
-[[Category: Park, S Y]]
+[[Category: Park S-Y]]
-[[Category: Tame, J R.H]]
+[[Category: Tame JRH]]
-[[Category: Autotransporter]]
-[[Category: Beta helix]]
-[[Category: Hydrolase]]
-[[Category: Mutant]]

3ak5

From Proteopedia

Current revision

Hemoglobin protease (Hbp) passenger missing domain-2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox