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1rg0
From Proteopedia
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| - | [[Image:1rg0.gif|left|200px]] | + | [[Image:1rg0.gif|left|200px]] |
| - | + | ||
| - | '''Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa''' | + | {{Structure |
| + | |PDB= 1rg0 |SIZE=350|CAPTION= <scene name='initialview01'>1rg0</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= PILA, FIMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa]) | ||
| + | }} | ||
| + | |||
| + | '''Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RG0 is a [ | + | 1RG0 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=1RG0 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 18: | Line 27: | ||
[[Category: adhesin]] | [[Category: adhesin]] | ||
[[Category: lectin]] | [[Category: lectin]] | ||
| - | [[Category: | + | [[Category: pseudomona]] |
[[Category: type iv pilin]] | [[Category: type iv pilin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:51:10 2008'' |
Revision as of 11:51, 20 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | PILA, FIMA (Pseudomonas aeruginosa) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa
Overview
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.
About this Structure
1RG0 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 13:51:10 2008
