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>

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>

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Revision as of 05:39, 29 March 2010 view source Elyse Yaremco (talk \| contribs) 52 edits No edit summary ← Older edit		Revision as of 05:41, 29 March 2010 view source Elyse Yaremco (talk \| contribs) 52 edits No edit summary Newer edit →
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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>