4Y9T

CRYSTAL STRUCTURE OF AN ABC TRANSPORTER SOLUTE BINDING PROTEIN (IPR025997) FROM AGROBACTERIUM VITIS S4 (Avi_5305, TARGET EFI-511224) WITH BOUND ALPHA-D-GLUCOSAMINE

Summary for 4Y9T

• Entry DOI: 10.2210/pdb4y9t/pdb
• Descriptor: ABC transporter, solute binding protein, 2-amino-2-deoxy-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: abc transporter solute binding protein, enzyme function initiative, efi, structural genomics, solute-binding protein
• Biological source: Agrobacterium vitis
• Total number of polymer chains: 1
• Total formula weight: 37614.08

Authors

Vetting, M.W.,Al Obaidi, N.F.,Toro, R.,Morisco, L.L.,Benach, J.,Koss, J.,Wasserman, S.R.,Attonito, J.D.,Scott Glenn, A.,Chamala, S.,Chowdhury, S.,Lafleur, J.,Love, J.,Seidel, R.D.,Whalen, K.L.,Gerlt, J.A.,Almo, S.C.,Enzyme Function Initiative (EFI) (deposition date: 2015-02-17, release date: 2015-03-11, Last modification date: 2024-11-13)

Primary citation

Yadava, U.,Vetting, M.W.,Al Obaidi, N.,Carter, M.S.,Gerlt, J.A.,Almo, S.C.
Structure of an ABC transporter solute-binding protein specific for the amino sugars glucosamine and galactosamine.
Acta Crystallogr.,Sect.F, 72:467-472, 2016

PubMed 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.

PubMed: 27303900
DOI: 10.1107/S2053230X16007500

Experimental method

X-RAY DIFFRACTION (1.801 Å)