Pilin: Difference between revisions

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==Structure==

Type IV pilin are homopolymers, composed of a single-chain pilin protein. A conserved 25 residue hydrophobic N terminal sequence is shared by all type IV pilins, as well as conserved pilus assembly machinery, and a unique N-methylated N-terminus. Type IVb pilins also contain a pair of conserved cysteines that form an intrachain disulphide bond<ref name=journal1>PMID:19626704</ref>. The cysteine-containing region in the C-terminus is thought to play function via the formation of disulfides in CFTR adhesion and in the assembly of PilS to make the pilus of the bacterium. The highly conserved N-terminal hydrophobic tail functions as a oligomerization domain for fibre formation.

Type IV pilin are homopolymers, composed of a single-chain pilin protein. A conserved 25 residue hydrophobic N terminal sequence is shared by all type IV pilins, as well as conserved pilus assembly machinery, and a unique N-methylated N-terminus. Type IVb pilins also contain a pair of conserved cysteines that form an intrachain disulphide bond <ref name=journal1>PMID:19626704</ref>.

~~Different protein folds for the type IVb pilins have been identified~~ <ref name=journal2>Asha M. Balakrishna,Yvonne Yih-Wan Tan, Henry Yu-Keung Mok,Anand M. Saxena,and Kunchithapadam Swaminathan. Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS. 2006 October 1; 62(Pt 10): 1024–1026</ref>.

The type IVb pilus operon of ''S. typhi'' contains the piLS gene, which encodes a structural pilin. The cysteine-containing region in the C-terminus is thought to play function via the formation of disulfides in CFTR adhesion and in the assembly of PilS to make the pilus of the bacterium. The highly conserved N-terminal hydrophobic tail functions as a oligomerization domain for fibre formation <ref name=journal2>Asha M. Balakrishna,Yvonne Yih-Wan Tan, Henry Yu-Keung Mok,Anand M. Saxena,and Kunchithapadam Swaminathan.

Different protein folds for the type IVb pilins have been identified Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS. 2006 October 1; 62(Pt 10): 1024–1026</ref>.

[[Image:N_Teeerminal_Hydrophobic.png|alt text]]

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 ==Structure==
-Type IV pilin are homopolymers, composed of a single-chain pilin protein. A conserved 25 residue hydrophobic N terminal sequence is shared by all type IV pilins, as well as conserved pilus assembly machinery, and a unique N-methylated N-terminus. Type IVb pilins also contain a pair of conserved cysteines that form an intrachain disulphide bond<ref name=journal1>PMID:19626704</ref>. The cysteine-containing region in the C-terminus is thought to play function via the formation of disulfides in CFTR adhesion and in the assembly of PilS to make the pilus of the bacterium. The highly conserved N-terminal hydrophobic tail functions as a oligomerization domain for fibre formation.
+Type IV pilin are homopolymers, composed of a single-chain pilin protein. A conserved 25 residue hydrophobic N terminal sequence is shared by all type IV pilins, as well as conserved pilus assembly machinery, and a unique N-methylated N-terminus. Type IVb pilins also contain a pair of conserved cysteines that form an intrachain disulphide bond <ref name=journal1>PMID:19626704</ref>.
-Different protein folds for the type IVb pilins have been identified <ref name=journal2>Asha M. Balakrishna,Yvonne Yih-Wan Tan, Henry Yu-Keung Mok,Anand M. Saxena,and Kunchithapadam Swaminathan. Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS. 2006 October 1; 62(Pt 10): 1024–1026</ref>.
+The type IVb pilus operon of ''S. typhi'' contains the piLS gene, which encodes a structural pilin. The cysteine-containing region in the C-terminus is thought to play function via the formation of disulfides in CFTR adhesion and in the assembly of PilS to make the pilus of the bacterium. The highly conserved N-terminal hydrophobic tail functions as a oligomerization domain for fibre formation <ref name=journal2>Asha M. Balakrishna,Yvonne Yih-Wan Tan, Henry Yu-Keung Mok,Anand M. Saxena,and Kunchithapadam Swaminathan.
+Different protein folds for the type IVb pilins have been identified  Crystallization and preliminary X-ray diffraction analysis of Salmonella typhi PilS. 2006 October 1; 62(Pt 10): 1024–1026</ref>.
 [[Image:N_Teeerminal_Hydrophobic.png|alt text]]