2ivw
From Proteopedia
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THE SOLUTION STRUCTURE OF A DOMAIN FROM THE NEISSERIA MENINGITIDIS PILP PILOT PROTEIN.
Overview
Type IV pili are long, thin fibres, which extend from the surface of the, bacterial pathogen Neisseria meningitidis; they play a key role in, adhesion and colonisation of host cells. PilP is a lipoprotein, suggested, to be involved in the assembly and stabilization of an outer membrane, protein, PilQ, which is required for pilus formation. Here we describe the, expression of a recombinant fragment of PilP, spanning residues 20 to 181, and determination of the solution structure of a folded domain, spanning, residues 85 to 163, by NMR. The N-terminal third of the protein, from, residues 20 to 84, is apparently unfolded. Protease digestion yielded a, 113 residue fragment that contained the folded domain. The domain adopts a, simple beta-sandwich type fold, consisting of a three-stranded beta-sheet, packed against a four-stranded beta-sheet. There is also a short segment, of 3(10) helix at the N-terminal part of the folded domain. We were unable, to identify any other proteins that are closely related in structure to, the PilP domain, although the fold appears to be distantly related to the, lipocalin family. Over 40 homologues of PilP have been identified in, Gram-negative bacteria and the majority of conserved residues lie within, the folded domain. The fourth beta-strand and adjacent loop regions, contain a high proportion of conserved residues, including three glycine, residues, which seem to play a role in linking the two beta-sheets. The, two beta-sheets pack together to form a crevice, lined with conserved, hydrophobic residues: we suggest that this feature could act as a binding, site for a small ligand. The results show that PilP and its homologues, have a conserved, folded domain at the C-terminal end of the protein that, may be involved in mediating binding to hydrophobic ligands.
About this Structure
2IVW is a Single protein structure of sequence from Neisseria meningitidis. Full crystallographic information is available from OCA.
Reference
The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new beta-sandwich fold., Golovanov AP, Balasingham S, Tzitzilonis C, Goult BT, Lian LY, Homberset H, Tonjum T, Derrick JP, J Mol Biol. 2006 Nov 24;364(2):186-95. Epub 2006 Sep 1. PMID:17007878
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