Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092

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• 作者：Simone Culurgioni ; Minzhe Tang and Martin Austin Walsh
• 关键词：Streptococcus pneumoniae ; substrate-binding protein SP0092 ; ABC transporters ; carbohydrate uptake
• 刊名：Acta Crystallographica Section F
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：73
• 期：1
• 页码：54-61
• 全文大小：2766K
• ISSN：1744-3091

文摘

Streptococcus pneumoniae is an opportunistic respiratory pathogen that remains a major cause of morbidity and mortality globally, with infants and the elderly at the highest risk. S. pneumoniae relies entirely on carbohydrates as a source of carbon and dedicates a third of all uptake systems to carbohydrate import. The structure of the carbohydrate-free substrate-binding protein SP0092 at 1.61 Å resolution reveals it to belong to the newly proposed subclass G of substrate-binding proteins, with a ligand-binding pocket that is large enough to accommodate complex oligosaccharides. SP0092 is a dimer in solution and the crystal structure reveals a domain-swapped dimer with the monomer subunits in a closed conformation but in the absence of carbohydrate ligand. This closed conformation may be induced by dimer formation and could be used as a mechanism to regulate carbohydrate uptake.