2QVC: Crystal Structure Of A Periplasmic Sugar Abc Transporter From Thermotoga Maritima

Citation:
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2012) 68 p.1460-1464
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 A resolution is reported. The molecule consists of two similar alpha/beta domains connected by a three-stranded hinge region. In the current structure, a ligand (beta-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.
PDB ID: 2QVCDownload
MMDB ID: 59558
PDB Deposition Date: 2007/8/8
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 2QVC: dimeric; determined by author and by software (PISA)
Molecular Components in 2QVC
Label Count Molecule
Proteins (2 molecules)
2
Sugar ABC Transporter, Periplasmic Sugar-binding Protein
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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