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Default Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.

Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.

Related Articles Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.

Sci Rep. 2013;3:1079

Authors: Wang T, Zhang J, Zhang X, Xu C, Tu X

Abstract
Streptococcus pneumoniae is a pathogen causing acute respiratory infection, otitis media and some other severe diseases in human. In this study, the solution structure of a bacterial immunoglobulin-like (Big) domain from a putative S. pneumoniae surface protein SP0498 was determined by NMR spectroscopy. SP0498 Big domain adopts an eight-?-strand barrel-like fold, which is different in some aspects from the two-sheet sandwich-like fold of the canonical Ig-like domains. Intriguingly, we identified that the SP0498 Big domain was a Ca(2+) binding domain. The structure of the Big domain is different from those of the well known Ca(2+) binding domains, therefore revealing a novel Ca(2+)-binding module. Furthermore, we identified the critical residues responsible for the binding to Ca(2+). We are the first to report the interactions between the Big domain and Ca(2+) in terms of structure, suggesting an important role of the Big domain in many essential calcium-dependent cellular processes such as pathogenesis.


PMID: 23326635 [PubMed - in process]



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