Structural highlights
FunctionPublication Abstract from PubMedThe serine rich repeat protein-1 (Srr-1) is an adhesive protein of Streptococcus agalactiae. It is the first bacterial protein identified to interact with human keratin 4 (K4 or KRT4). Within Srr-1, the residues 311-641 constitute the non-repeat ligand binding region (Srr-1-BR311-641). The C-terminal part of Srr-1-BR311-641, comprising of residues 485-642 (termed Srr-1-K4BD), have been identified to bind to K4. Here we report the crystal structure of recombinant Srr-1-K4BD485-642 and its possible mode of interaction with K4 through docking studies. The dimeric structure of Srr-1-K4BD485-642 reveals a novel two way "slide lock" parallel beta-sheet complementation where the C-terminal strand of one monomer is positioned anti-parallel to the N-terminal strand of the adjacent monomer and this arrangement is not seen so far in any of the homologous structures. The dimerization of Srr-1-K4BD485-642 observed both in the crystal structure and in solution suggests that similar domain association could also be possible in in vivo and we propose this association would likely generate a new binding site for another host molecule. It is likely that the adhesin can recognize multiple ligands using its ligand binding sub-domains through their intra and inter domain association with one another. Structure of KRT4 binding domain of Srr-1 from Streptococcus agalactiae reveals a novel beta-sheet complementation.,Sundaresan R, Samen U, Ponnuraj K Int J Biol Macromol. 2015 Jan 17;75C:97-105. doi: 10.1016/j.ijbiomac.2014.12.048. PMID:25603146[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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