4jso

The X-ray crystal structure of a thermophilic cellobiose binding protein bound with laminaripentaose

spinqualitylabelsall models 4jso, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jso is a 1 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.07Å Ligands: BGC, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9WXN8_THEMA Publication Abstract from PubMed 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 important implications in ligand binding and drug design studies. We sought to investigate the determinants of ligand binding selectivity in tmCBP through biophysical characterization of tmCBP in the presence of varying beta-glucan oligosaccharides. Crystal structures show that whilst the amino acids that comprise both the tmCBP subsite one and subsite two binding sites remain fixed in conformation regardless of which ligands are present, the rich hydrogen bonding potential of water molecules may facilitate the ordering and the plasticity of this unique PBP binding site. CONCLUSIONS: The identification of the roles these water molecules play in ligand recognition suggests potential mechanisms that can be utilized to adapt a single ligand binding site to recognize multiple distinct ligands. Molecular details of ligand selectivity determinants in a promiscuous beta-glucan periplasmic binding protein.,Munshi P, Stanley CB, Ghimire-Rijal S, Lu X, Myles DA, Cuneo MJ BMC Struct Biol. 2013 Oct 4;13:18. doi: 10.1186/1472-6807-13-18. PMID:24090243 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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