Pilin: Difference between revisions

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192 water molecules and 2107 non-hydrogen atoms are found in the native structure of PilS and the loop regions of this protein are highly flexible. The crystal structure of PilS contains the standard αβ fold of the type IVb pilin, with a central anti-parallel β-sheet platform that is made up of seven β strands, and surrounded by four α helices. The complete β sheet topology of PilS is β1-β2-β3-β4-β7-β5-β6. <ref name=journal1>PMID:19626704</ref> The N-terminal alpha helix (α1) can be found on three of these strands (β3, β4, and β7).The alpha helix of the type IVb pilins is straight, as there is no proline or glycine present in positions that would disturb the structure of the helix. The region between the N-terminal alpha helix and β3 (the αβ-loop) contains another alpha helix (α2) and also a pair of anti-parallel β-strands (β1 and β2). Helix α2 packs almost perpendicular to and on top of helix α1, causing helix α2, strand β1, and the α1-α2 loop of PilS to be all located on one side of the molecule. Finally, a disulfide bridge links the residues Cys126 and Cys 163. <ref name=journal1>PMID:19626704</ref>
192 water molecules and 2107 non-hydrogen atoms are found in the native structure of PilS and the loop regions of this protein are highly flexible. The crystal structure of PilS contains the standard αβ fold of the type IVb pilin, with a central anti-parallel β-sheet platform that is made up of seven β strands, and surrounded by four α helices. The complete β sheet topology of PilS is β1-β2-β3-β4-β7-β5-β6. <ref name=journal1>PMID:19626704</ref> The N-terminal alpha helix (α1) can be found on three of these strands (β3, β4, and β7).The alpha helix of the type IVb pilins is straight, as there is no proline or glycine present in positions that would disturb the structure of the helix. The region between the N-terminal alpha helix and β3 (the αβ-loop) contains another alpha helix (α2) and also a pair of anti-parallel β-strands (β1 and β2). Helix α2 packs almost perpendicular to and on top of helix α1, causing helix α2, strand β1, and the α1-α2 loop of PilS to be all located on one side of the molecule. Finally, a disulfide bridge links the residues Cys126 and Cys 163. <ref name=journal1>PMID:19626704</ref>
The final model of the PilS complex structure consists of a dimer of 149 amino acid residues of each monomer and the 10-mer peptide and 262 water molecules.  The movement of two lysine side chains in the complex structure function to bind the peptide by making ionic contacts (formation of salt bridges) with the negatively charged residues of the CFTR peptide.<ref name=journal1>PMID:19626704</ref>
The final model of the PilS complex structure consists of a dimer of 149 amino acid residues of each monomer and the 10-mer peptide and 262 water molecules.  The movement of two lysine side chains in the complex structure function to bind the peptide by making ionic contacts (formation of salt bridges) with the negatively charged residues of the CFTR peptide.<ref name=journal1>PMID:19626704</ref>
                   
 
 
                   
==Function==
==Function==


Type IV pili are diverse in function; they mediate numerous cellular functions via their polymeric machinery. These functions include cell adhesion, signalling, phage attachment, surface motility, biofilm formation and DNA uptake by natural transformation. Specifically, the type IVb pilus of ''Salmonella typhi'' is the adhesion factor that allows the pathogen to enter into the gastrointestinal cells of humans with ease. The first step in ''S.typhi'' pathogenesis is the type IVb pilus self-mediated self-association in the anerobic human small intestine preceding the entry into the human intestine epithelium. <ref name=journal1>PMID:19626704</ref>
Type IV pili are diverse in function; they mediate numerous cellular functions via their polymeric machinery. These functions include cell adhesion, signalling, phage attachment, surface motility, biofilm formation and DNA uptake by natural transformation. Specifically, the type IVb pilus of ''Salmonella typhi'' is the adhesion factor that allows the pathogen to enter into the gastrointestinal cells of humans with ease. The first step in ''S.typhi'' pathogenesis is the type IVb pilus self-mediated self-association in the anerobic human small intestine preceding the entry into the human intestine epithelium. <ref name=journal1>PMID:19626704</ref>
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|


===pilin===
*pilin


[[3fhu]]  – StPrePIL type IV b residues 26-181 – ''Salmonella typhii''<BR />
**[[3fhu]]  – StPrePIL type IV b residues 26-181 – ''Salmonella typhii''<BR />
[[1q5f]] - StPrePIL type IV b residues 26-181 - NMR<BR />
**[[1q5f]] - StPrePIL type IV b residues 26-181 - NMR<BR />
[[1kb7]], [[1kb8]] – PaPIL KB7 – ''Pseudomonas aeruginosa'' – NMR<BR />
**[[1kb7]], [[1kb8]] – PaPIL KB7 – ''Pseudomonas aeruginosa'' – NMR<BR />
[[1nil]], [[1nim]] - PaPIL PAK – NMR<BR />
**[[1nil]], [[1nim]] - PaPIL PAK – NMR<BR />
[[1oqw]], [[1x6p]], [[1x6q]], [[1x6r]], [[1x6z]], [[1x6x]], [[1x6y]] - PaPIL PAK<BR />
**[[1oqw]], [[1x6p]], [[1x6q]], [[1x6r]], [[1x6z]], [[1x6x]], [[1x6y]] - PaPIL PAK<BR />
[[2py0]] - PaPIL PAK (mutant) <BR />
**[[2py0]] - PaPIL PAK (mutant) <BR />
[[1pan]], [[1pao]] - PaPIL PAO – NMR<BR />
**[[1pan]], [[1pao]] - PaPIL PAO – NMR<BR />
[[1hpw]], [[1qve]], [[1rg0]] – PaPIL residues 29-150<BR />
**[[1hpw]], [[1qve]], [[1rg0]] – PaPIL residues 29-150<BR />
[[1ay2]], [[2pil]], [[2hi2]], [[2hil]] – PIL type IV – ''Neisseria gonorrhoeae''<BR />
**[[1ay2]], [[2pil]], [[2hi2]], [[2hil]] – PIL type IV – ''Neisseria gonorrhoeae''<BR />
[[2m3k]] - PIL type IV – ''Neisseria meningitis'' – NMR<br />
**[[2m3k]] - PIL type IV – ''Neisseria meningitis'' – NMR<br />
[[1dzo]] - PaPIL type IV globular domain (mutant) <BR />
**[[1dzo]] - PaPIL type IV globular domain (mutant) <BR />
[[3jyz]], [[3jzz]] - PaPIL type IV globular domain<BR />
**[[3jyz]], [[3jzz]] - PaPIL type IV globular domain<BR />
[[2j6r]], [[3gea]], [[3ggh]], [[3hlr]] – EcPIL K88<BR />
**[[2j6r]], [[3gea]], [[3ggh]], [[3hlr]] – EcPIL K88<BR />
[[2jty]] – EcPIL type IA<BR />
**[[2jty]] – EcPIL type IA<BR />
[[2m5g]] - EcPIL type IA – NMR<br />
**[[2m5g]] - EcPIL type IA – NMR<br />
[[3s0t]] - EcPIL type IV<br />
**[[3s0t]] - EcPIL type IV<br />
[[3gld]], [[3gle]] – PIL (mutant) – ''Streptococcus pyogenes''<BR />
**[[3gld]], [[3gle]] – PIL (mutant) – ''Streptococcus pyogenes''<BR />
[[3f83]], [[3f84]], [[3f85]] – EcPIL CFAE/CFAB<br />
**[[3f83]], [[3f84]], [[3f85]] – EcPIL CFAE/CFAB<br />
[[3vor]] - EcPIL CFA/III<br />
**[[3vor]] - EcPIL CFA/III<br />
[[4bhr]] - TtPIL type IV – ''Thermus thermophilus''<br />
**[[4bhr]] - TtPIL type IV – ''Thermus thermophilus''<br />
[[4ixj]] - PIL type IV – ''Clostridium difficile''<br />
**[[4ixj]] - PIL type IV – ''Clostridium difficile''<br />


===Pilin binary complex===
*Pilin binary complex


[[3fhv]] - StPrePIL  type IV b residues 26-181 + CFTR peptide<BR />
**[[3fhv]] - StPrePIL  type IV b residues 26-181 + CFTR peptide<BR />
[[3gew]] - EcPIL K88 + chaperone protein FAEE<BR />
**[[3gew]] - EcPIL K88 + chaperone protein FAEE<BR />
[[2xg4]], [[2xg5]], [[2j2z]] - EcPIL PAP + chaperone protein PAPD<BR />
**[[2xg4]], [[2xg5]], [[2j2z]] - EcPIL PAP + chaperone protein PAPD<BR />
[[2w07]], [[2uy6]], [[2uy7]] – EcPIL PAPF (mutant) + chaperone protein PAPD<br />
**[[2w07]], [[2uy6]], [[2uy7]] – EcPIL PAPF (mutant) + chaperone protein PAPD<br />
[[3sqb]], [[4dwh]] - EcPIL type 1A + chaperone protein FIMC<br />
**[[3sqb]], [[4dwh]] - EcPIL type 1A + chaperone protein FIMC<br />
   
  }}
   
   


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