Molecular details of ligand selectivity determinants in a promiscuous β-glucan periplasmic binding protein.

ABSTRACT:

Background

Members of the periplasmic binding protein (PBP) superfamily utilize a highly conserved inter-domain ligand binding site that adapts to specifically bind a chemically diverse range of ligands. This paradigm of PBP ligand binding specificity was recently altered when the structure of the Thermotoga maritima cellobiose-binding protein (tmCBP) was solved. The tmCBP binding site is bipartite, comprising a canonical solvent-excluded region (subsite one), adjacent to a solvent-filled cavity (subsite two) where specific and semi-specific ligand recognition occur, respectively.

Results

A molecular level understanding of binding pocket adaptation mechanisms that simultaneously allow both ligand specificity at subsite one and promiscuity at subsite two has potentially impor

SUBMITTER: Munshi P 

PROVIDER: S-EPMC3850815 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature