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Structure of a periplasmic glucose-binding protein from Thermotoga maritima.

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 ?/? domains connected by a three-stranded hinge region. In the current structure, a ligand (?-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.

SUBMITTER: Palani K

PROVIDER: S-EPMC3509965 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Structure of a periplasmic glucose-binding protein from Thermotoga maritima.

Palani Kandavelu K Kumaran Desigan D Burley Stephen K SK Swaminathan Subramanyam S

Acta crystallographica. Section F, Structural biology and crystallization communications 20121119 Pt 12

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 ligan ...[more]

PMID: 23192024

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Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein.

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The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima.

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Crystal structure of the cell division protein FtsA from Thermotoga maritima.

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Cryo-EM Structure of Heterologous Protein Complex Loaded Thermotoga Maritima Encapsulin Capsid.

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Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima.

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