Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 75, Issue -, Pages 97-105Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2014.12.048
Keywords
Adhesin; Keratin-binding; beta-sheet complementation
Funding
- Department of Biotechnology (DBT), Government of India
- University Grants Commission (UGC), Government of India
- Department of Science and Technology (DST), Government of India
- Ministry of Foreign Affairs/Sincrotrone Trieste (MAE), Italy
- International Centre for Theoretical Physics (ICTP), Trieste, Italy
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The 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 (1(4 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-K4BD(485-642) and its possible mode of interaction with 1(4 through docking studies. The dimeric structure of Srr-1-K4BD(485-642) 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-K4BD(455-642) 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. (C) 2015 Elsevier B.V. All rights reserved.
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