» Articles » PMID: 27303900

Structure of an ABC Transporter Solute-binding Protein Specific for the Amino Sugars Glucosamine and Galactosamine

Overview
Specialty Chemistry
Date 2016 Jun 16
PMID 27303900
Citations 2
Authors
Affiliations
Soon will be listed here.
Abstract

The uptake of exogenous solutes by prokaryotes is mediated by transport systems embedded in the plasma membrane. In many cases, a solute-binding protein (SBP) is utilized to bind ligands with high affinity and deliver them to the membrane-bound components responsible for translocation into the cytoplasm. In the present study, Avi_5305, an Agrobacterium vitis SBP belonging to Pfam13407, was screened by differential scanning fluorimetry (DSF) and found to be stabilized by D-glucosamine and D-galactosamine. Avi_5305 is the first protein from Pfam13407 shown to be specific for amino sugars, and co-crystallization resulted in structures of Avi_5305 bound to D-glucosamine and D-galactosamine. Typical of Pfam13407, Avi_5305 consists of two α/β domains linked through a hinge region, with the ligand-binding site located in a cleft between the two domains. Comparisons with Escherichia coli ribose-binding protein suggest that a cation-π interaction with Tyr168 provides the specificity for D-glucosamine/D-galactosamine over D-glucose/D-galactose.

Citing Articles

In-silico molecular designs to treat neurologic and ophthalmologic diseases caused by sorbitol excess: engineering the Agrobacterium vitis protein.

Sharma S, Hojati A, Gnanasambandam B, Yerrabelli R, Brozek J BMC Res Notes. 2023; 16(1):129.

PMID: 37400926 PMC: 10318746. DOI: 10.1186/s13104-023-06367-2.


The Fish Pathogen Aliivibrio salmonicida LFI1238 Can Degrade and Metabolize Chitin despite Gene Disruption in the Chitinolytic Pathway.

Skane A, Minniti G, Loose J, Mekasha S, Bissaro B, Mathiesen G Appl Environ Microbiol. 2021; 87(19):e0052921.

PMID: 34319813 PMC: 8432520. DOI: 10.1128/AEM.00529-21.

References
1.
Krissinel E, Henrick K . Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr. 2004; 60(Pt 12 Pt 1):2256-68. DOI: 10.1107/S0907444904026460. View

2.
Curtis S, Epstein W . Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase. J Bacteriol. 1975; 122(3):1189-99. PMC: 246176. DOI: 10.1128/jb.122.3.1189-1199.1975. View

3.
Bendtsen J, Nielsen H, von Heijne G, Brunak S . Improved prediction of signal peptides: SignalP 3.0. J Mol Biol. 2004; 340(4):783-95. DOI: 10.1016/j.jmb.2004.05.028. View

4.
Michalska K, Chang C, Mack J, Zerbs S, Joachimiak A, Collart F . Characterization of transport proteins for aromatic compounds derived from lignin: benzoate derivative binding proteins. J Mol Biol. 2012; 423(4):555-75. PMC: 3836681. DOI: 10.1016/j.jmb.2012.08.017. View

5.
Schumacher M, Choi K, ZALKIN H, Brennan R . Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices. Science. 1994; 266(5186):763-70. DOI: 10.1126/science.7973627. View