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| - | [[Image:1ji4.gif|left|200px]] | |
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| - | {{Structure
| + | ==NAP protein from helicobacter pylori== |
| - | |PDB= 1ji4 |SIZE=350|CAPTION= <scene name='initialview01'>1ji4</scene>, resolution 2.52Å
| + | <StructureSection load='1ji4' size='340' side='right'caption='[[1ji4]], [[Resolution|resolution]] 2.52Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene> | + | <table><tr><td colspan='2'>[[1ji4]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JI4 FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.52Å</td></tr> |
| - | |GENE= NAPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])
| + | <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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> |
| - | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ji4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ji4 OCA], [https://pdbe.org/1ji4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ji4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ji4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ji4 ProSAT]</span></td></tr> |
| - | |RELATEDENTRY=[[1dps|1DPS]], [[1qgh|1QGH]]
| + | </table> |
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ji4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ji4 OCA], [http://www.ebi.ac.uk/pdbsum/1ji4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ji4 RCSB]</span>
| + | == Function == |
| - | }}
| + | [https://www.uniprot.org/uniprot/DPS_HELPY DPS_HELPY] Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). Required for the survival in the presence of oxidative stress. Dps is also a virulence factor that activates neutrophils, mast cells and monocytes. It binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. It might have a role in the accumulation of neutrophils and monocytes at the site of infection. Induces superoxide anion generation, adhesion and chemotaxis of neutrophils, through a pertussis toxin-sensitive pathway involving MAP kinases.<ref>PMID:11069248</ref> <ref>PMID:7768601</ref> <ref>PMID:10790422</ref> <ref>PMID:11857341</ref> <ref>PMID:12672049</ref> <ref>PMID:12748264</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/1ji4_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ji4 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Helicobacter pylori is a major human pathogen associated with severe gastroduodenal diseases, including ulcers and cancers. An H.pylori protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophils. In order to achieve a molecular understanding of its unique immunogenic and pro-inflammatory properties, we have determined its three-dimensional structure. Its quaternary structure is similar to that of the dodecameric bacterial ferritins (Dps-like family), but it has a different surface potential charge distribution. This is due to the presence of a large number of positively charged residues, which could well account for its unique ability in activating human leukocytes. |
| | | | |
| - | '''NAP protein from helicobacter pylori'''
| + | Structure of the neutrophil-activating protein from Helicobacter pylori.,Zanotti G, Papinutto E, Dundon W, Battistutta R, Seveso M, Giudice G, Rappuoli R, Montecucco C J Mol Biol. 2002 Oct 11;323(1):125-30. PMID:12368104<ref>PMID:12368104</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 1ji4" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Overview== | + | ==See Also== |
| - | Helicobacter pylori is a major human pathogen associated with severe gastroduodenal diseases, including ulcers and cancers. An H.pylori protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophils. In order to achieve a molecular understanding of its unique immunogenic and pro-inflammatory properties, we have determined its three-dimensional structure. Its quaternary structure is similar to that of the dodecameric bacterial ferritins (Dps-like family), but it has a different surface potential charge distribution. This is due to the presence of a large number of positively charged residues, which could well account for its unique ability in activating human leukocytes.
| + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| - | | + | == References == |
| - | ==About this Structure==
| + | <references/> |
| - | 1JI4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JI4 OCA].
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==Reference== | + | |
| - | Structure of the neutrophil-activating protein from Helicobacter pylori., Zanotti G, Papinutto E, Dundon W, Battistutta R, Seveso M, Giudice G, Rappuoli R, Montecucco C, J Mol Biol. 2002 Oct 11;323(1):125-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12368104 12368104]
| + | |
| | [[Category: Helicobacter pylori]] | | [[Category: Helicobacter pylori]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Battistutta, R.]] | + | [[Category: Battistutta R]] |
| - | [[Category: Dundon, W G.]] | + | [[Category: Del Giudice G]] |
| - | [[Category: Giudice, G Del.]] | + | [[Category: Dundon WG]] |
| - | [[Category: Montecucco, C.]] | + | [[Category: Montecucco C]] |
| - | [[Category: Papinutto, E.]] | + | [[Category: Papinutto E]] |
| - | [[Category: Rappuoli, R.]] | + | [[Category: Rappuoli R]] |
| - | [[Category: Seveso, M.]] | + | [[Category: Seveso M]] |
| - | [[Category: Zanotti, G.]] | + | [[Category: Zanotti G]] |
| - | [[Category: dodecamer]]
| + | |
| - | [[Category: four-helix bundle]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:33:59 2008''
| + | |
| Structural highlights
Function
DPS_HELPY Protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction (By similarity). Required for the survival in the presence of oxidative stress. Dps is also a virulence factor that activates neutrophils, mast cells and monocytes. It binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. It might have a role in the accumulation of neutrophils and monocytes at the site of infection. Induces superoxide anion generation, adhesion and chemotaxis of neutrophils, through a pertussis toxin-sensitive pathway involving MAP kinases.[1] [2] [3] [4] [5] [6]
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
Helicobacter pylori is a major human pathogen associated with severe gastroduodenal diseases, including ulcers and cancers. An H.pylori protein that is highly immunogenic in humans and mice has been identified recently. This protein has been termed HP-NAP, due to its ability of activating neutrophils. In order to achieve a molecular understanding of its unique immunogenic and pro-inflammatory properties, we have determined its three-dimensional structure. Its quaternary structure is similar to that of the dodecameric bacterial ferritins (Dps-like family), but it has a different surface potential charge distribution. This is due to the presence of a large number of positively charged residues, which could well account for its unique ability in activating human leukocytes.
Structure of the neutrophil-activating protein from Helicobacter pylori.,Zanotti G, Papinutto E, Dundon W, Battistutta R, Seveso M, Giudice G, Rappuoli R, Montecucco C J Mol Biol. 2002 Oct 11;323(1):125-30. PMID:12368104[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Leakey A, La Brooy J, Hirst R. The ability of Helicobacter pylori to activate neutrophils is determined by factors other than H. pylori neutrophil-activating protein. J Infect Dis. 2000 Dec;182(6):1749-55. Epub 2000 Oct 26. PMID:11069248 doi:http://dx.doi.org/JID000555
- ↑ Evans DJ Jr, Evans DG, Takemura T, Nakano H, Lampert HC, Graham DY, Granger DN, Kvietys PR. Characterization of a Helicobacter pylori neutrophil-activating protein. Infect Immun. 1995 Jun;63(6):2213-20. PMID:7768601
- ↑ Satin B, Del Giudice G, Della Bianca V, Dusi S, Laudanna C, Tonello F, Kelleher D, Rappuoli R, Montecucco C, Rossi F. The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a protective antigen and a major virulence factor. J Exp Med. 2000 May 1;191(9):1467-76. PMID:10790422
- ↑ Montemurro P, Nishioka H, Dundon WG, de Bernard M, Del Giudice G, Rappuoli R, Montecucco C. The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a potent stimulant of mast cells. Eur J Immunol. 2002 Mar;32(3):671-6. PMID:11857341 doi:http://dx.doi.org/10.1002/1521-4141(200203)32:3<671::AID-IMMU671>3.0.CO;2-5
- ↑ Nishioka H, Baesso I, Semenzato G, Trentin L, Rappuoli R, Del Giudice G, Montecucco C. The neutrophil-activating protein of Helicobacter pylori (HP-NAP) activates the MAPK pathway in human neutrophils. Eur J Immunol. 2003 Apr;33(4):840-9. PMID:12672049 doi:http://dx.doi.org/10.1002/eji.200323726
- ↑ Cooksley C, Jenks PJ, Green A, Cockayne A, Logan RP, Hardie KR. NapA protects Helicobacter pylori from oxidative stress damage, and its production is influenced by the ferric uptake regulator. J Med Microbiol. 2003 Jun;52(Pt 6):461-9. PMID:12748264
- ↑ Zanotti G, Papinutto E, Dundon W, Battistutta R, Seveso M, Giudice G, Rappuoli R, Montecucco C. Structure of the neutrophil-activating protein from Helicobacter pylori. J Mol Biol. 2002 Oct 11;323(1):125-30. PMID:12368104
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