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| | ==Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa== | | ==Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa== |
| - | <StructureSection load='1rg0' size='340' side='right' caption='[[1rg0]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='1rg0' size='340' side='right'caption='[[1rg0]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rg0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RG0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RG0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rg0]] 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=1RG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RG0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qve|1qve]], [[1hpw|1hpw]], [[1dzo|1dzo]], [[1oqw|1oqw]], [[1ayz|1ayz]], [[1oqv|1oqv]]</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]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PILA, FIMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=1rg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rg0 OCA], [https://pdbe.org/1rg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rg0 RCSB], [https://www.ebi.ac.uk/pdbsum/1rg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rg0 ProSAT]</span></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=1rg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rg0 OCA], [http://pdbe.org/1rg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rg0 RCSB], [http://www.ebi.ac.uk/pdbsum/1rg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rg0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FMP1_PSEAI FMP1_PSEAI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Pilin|Pilin]] | + | *[[Pilin 3D structures|Pilin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Audette, G F]] | + | [[Category: Large Structures]] |
| - | [[Category: Hazes, B]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Irvin, R T]] | + | [[Category: Audette GF]] |
| - | [[Category: Adhesin]] | + | [[Category: Hazes B]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Irvin RT]] |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Pseudomona]]
| + | |
| - | [[Category: Type iv pilin]]
| + | |
| Structural highlights
Function
FMP1_PSEAI
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
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Audette GF, Irvin RT, Hazes B. Crystallographic analysis of the Pseudomonas aeruginosa strain K122-4 monomeric pilin reveals a conserved receptor-binding architecture. Biochemistry. 2004 Sep 14;43(36):11427-35. PMID:15350129 doi:http://dx.doi.org/10.1021/bi048957s
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