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1qve

From Proteopedia

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{{Seed}}
 
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[[Image:1qve.png|left|200px]]
 
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==Crystal structure of the truncated K122-4 pilin from Pseudomonas aeruginosa==
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The line below this paragraph, containing "STRUCTURE_1qve", creates the "Structure Box" on the page.
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<StructureSection load='1qve' size='340' side='right'caption='[[1qve]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qve]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QVE FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.54&#8491;</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=1qve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qve OCA], [https://pdbe.org/1qve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qve RCSB], [https://www.ebi.ac.uk/pdbsum/1qve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qve ProSAT]</span></td></tr>
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{{STRUCTURE_1qve| PDB=1qve | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FMP1_PSEAI FMP1_PSEAI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qv/1qve_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1qve ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Adherence of pathogens to host cells is critical for the initiation of infection and is thus an attractive target for anti-infective therapeutics and vaccines. In the opportunistic human pathogen Pseudomonas aeruginosa, host-cell adherence is achieved predominantly by type IV pili. Analysis of several clinical strains of P. aeruginosa reveals poor sequence conservation between pilin genes, including the residues in the receptor-binding site. Interestingly, the receptor-binding sites appear to retain a conserved surface epitope because all Pseudomonas type IV pili recognize the same receptor on the host cell and cross-reactive antibodies specific for the receptor-binding site exist. Here, we present the crystallographic analysis of two crystal forms of truncated pilin from P. aeruginosa strain K122-4 (DeltaK122-4) at 1.54 and 1.8 A resolution, respectively. The DeltaK122-4 structure is compared to other crystallographically determined type IV pilin structures and an NMR structure of DeltaK122-4 pilin. A comparison with the structure of the highly divergent P. aeruginosa strain K (DeltaPAK) pilin indicates that the receptor-binding loop in both pilins forms a shallow depression with a surface that is formed by main-chain atoms. Conservation of this putative binding site is independent of the sequence as long as the main-chain conformation is conserved and could therefore explain the shared receptor specificity and antibody cross reactivity of highly divergent Pseudomonas type IV pilins.
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===Crystal structure of the truncated K122-4 pilin from Pseudomonas aeruginosa===
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Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture.,Audette GF, Irvin RT, Hazes B Biochemistry. 2004 Sep 14;43(36):11427-35. PMID:15350129<ref>PMID:15350129</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 1qve" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15350129}}, adds the Publication Abstract to the page
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*[[Pilin 3D structures|Pilin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15350129 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15350129}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1QVE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVE OCA].
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==Reference==
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Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture., Audette GF, Irvin RT, Hazes B, Biochemistry. 2004 Sep 14;43(36):11427-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15350129 15350129]
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Single protein]]
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[[Category: Audette GF]]
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[[Category: Audette, G F.]]
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[[Category: Hazes B]]
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[[Category: Hazes, B.]]
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[[Category: Irvin RT]]
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[[Category: Irvin, R T.]]
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[[Category: Adhesin]]
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[[Category: Lectin]]
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[[Category: Pseudomona]]
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[[Category: Type iv pilin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:28:01 2008''
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Current revision

Crystal structure of the truncated K122-4 pilin from Pseudomonas aeruginosa

PDB ID 1qve

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