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Title: Structural Basis for a Ribofuranosyl Binding Protein: Insights into the Furanose Specific Transport

The ATP-binding cassette transporters (ABC-transporters) are members of one of the largest protein superfamilies, with representatives in all extant phyla. These integral membrane proteins utilize the energy of ATP hydrolysis to carry out certain biological processes, including translocation of various substrates across membranes and non-transport related processes such as translation of RNA and DNA repair. Typically, such transport systems in bacteria consist of an ATP binding component, a transmembrane permease, and a periplasmic receptor or binding protein. Soluble proteins found in the periplasm of gram-negative bacteria serve as the primary receptors for transport of many compounds, such as sugars, small peptides, and some ions. Ligand binding activates these periplasmic components, permitting recognition by the membrane spanning domain, which supports for transport and, in some cases, chemotaxis. Transport and chemotaxis processes appear to be independent of one another, and a few mutants of bifunctional periplasmic components reveal the absence of one or the other function. Previously published high-resolution X-ray structures of various periplasmic ligand binding proteins include Arabinose binding protein (ABP), Allose binding protein (ALBP), Glucose-galactose binding protein (GBP) and Ribose binding protein (RBP). Each of these proteins consists of two structurally similar domains connected by a three-stranded hinge region, withmore » ligand buried between the domains. Upon ligand binding and release, various conformational changes have been observed. For RBP, open (apo) and closed (ligand bound) conformations have been reported and so for MBP. The closed/active form of the protein interacts with the integral membrane component of the system in both transport and chemotaxis. Herein, we report 1.9{angstrom} resolution X-ray structure of the R{sub f}BP periplasmic component of an ABC-type sugar transport system from Hahella chejuensis (UniProt Id Q2S7D2) bound to the unusual furanose form of ribose.« less
Authors:
; ; ;
Publication Date:
OSTI Identifier:
1040557
Report Number(s):
BNL--95087-2011-JA
Journal ID: ISSN 0887-3585; PSFGEY; 600301010; TRN: US201210%%733
DOE Contract Number:
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Proteins; Journal Volume: 79; Journal Issue: 4
Research Org:
BROOKHAVEN NATIONAL LABORATORY (BNL)
Sponsoring Org:
ELI LILLY & COMPANY
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; ARABINOSE; BACTERIA; CONFORMATIONAL CHANGES; DNA REPAIR; HYDROLYSIS; MEMBRANE PROTEINS; MEMBRANES; MUTANTS; PEPTIDES; PROTEINS; RESOLUTION; RIBOSE; RNA; SACCHARIDES; SACCHAROSE; SUBSTRATES; TRANSLOCATION; TRANSPORT nanolipoprotein particles; nanodiscs; fluorescence correlation spectroscopy; membrane proteins