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| - | [[Image:1rg0.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1rg0.png|left|200px]] |
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| | {{STRUCTURE_1rg0| PDB=1rg0 | SCENE= }} | | {{STRUCTURE_1rg0| PDB=1rg0 | SCENE= }} |
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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=== |
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| - | ==Overview==
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15350129}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15350129 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15350129}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pseudomona]] | | [[Category: Pseudomona]] |
| | [[Category: Type iv pilin]] | | [[Category: Type iv pilin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:27:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:28:49 2008'' |
Revision as of 03:28, 29 July 2008
Template:STRUCTURE 1rg0
Monoclinic crystal form of the truncated K122-4 pilin from Pseudomonas aeruginosa
Template:ABSTRACT PUBMED 15350129
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 Tue Jul 29 06:28:49 2008
