2QVC

Crystal structure of a periplasmic sugar ABC transporter from Thermotoga maritima

Summary for 2QVC

• Entry DOI: 10.2210/pdb2qvc/pdb
• Descriptor: Sugar ABC transporter, periplasmic sugar-binding protein, beta-D-glucopyranose (3 entities in total)
• Functional Keywords: abc sugar transporter, sugar-binding protein, protein structure initiative ii, psi ii, nysgxrc, 11013q, structural genomics, new york sgx research center for structural genomics, transport protein
• Biological source: Thermotoga maritima MSB8
• Total number of polymer chains: 4
• Total formula weight: 138511.34

Authors

Palani, K.,Kumaran, D.,Burley, S.K.,Swaminathan, S.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2007-08-08, release date: 2007-08-28, Last modification date: 2024-10-30)

Primary citation

Palani, K.,Kumaran, D.,Burley, S.K.,Swaminathan, S.
Structure of a periplasmic glucose-binding protein from Thermotoga maritima.
Acta Crystallogr.,Sect.F, 68:1460-1464, 2012

PubMed Abstract: ABC transport systems have been characterized in organisms ranging from bacteria to humans. In most bacterial systems, the periplasmic component is the primary determinant of specificity of the transport complex as a whole. Here, the X-ray crystal structure of a periplasmic glucose-binding protein (GBP) from Thermotoga maritima determined at 2.4 Å resolution is reported. The molecule consists of two similar α/β domains connected by a three-stranded hinge region. In the current structure, a ligand (β-D-glucose) is buried between the two domains, which have adopted a closed conformation. Details of the substrate-binding sites revealed features that determine substrate specificity. In toto, ten residues from both domains form eight hydrogen bonds to the bound sugar and four aromatic residues (two from each domain) stabilize the substrate through stacking interactions.

PubMed: 23192024
DOI: 10.1107/S1744309112045241

Experimental method

X-RAY DIFFRACTION (2.4 Å)