Literature DB >> 23722846

Expression, crystallization and preliminary crystallographic study of GluB from Corynebacterium glutamicum.

Qingbo Liu1, Defeng Li, Yonglin Hu, Da Cheng Wang.   

Abstract

GluB is a substrate-binding protein (SBP) which participates in the uptake of glutamic acid in Corynebacterium glutamicum, a Gram-positive bacterium. It is part of an ATP-binding cassette (ABC) transporter system. Together with the transmembrane proteins GluC and GluD and the cytoplasmic protein GluA, which couples the hydrolysis of ATP to the translocation of glutamate, they form a highly active glutamate-uptake system. As part of efforts to study the amino-acid metabolism, especially the metabolism of glutamic acid by C. glutamicum, a bacterium that is widely used in the industrial production of glutamic acid, the GluB protein was expressed, purified and crystallized, an X-ray diffraction data set was collected to a resolution of 1.9 Å and preliminary crystallographic analysis was performed. The crystal belonged to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 82.50, c = 72.69 Å.

Entities:  

Keywords:  Corynebacterium glutamicum; glutamic acid binding protein; glutamic acid metabolism

Mesh:

Substances:

Year:  2013        PMID: 23722846      PMCID: PMC3668587          DOI: 10.1107/S1744309113011652

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  10 in total

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Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2005-12-14

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10.  A bacterial virulence factor with a dual role as an adhesin and a solute-binding protein: the crystal structure at 1.5 A resolution of the PEB1a protein from the food-borne human pathogen Campylobacter jejuni.

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  10 in total

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