Related ArticlesSolution 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.
[NMR paper] Solution Structure, Dynamics and Binding Studies of a Family 11 Carbohydrate-Binding Module from Clostridium thermocellum (CtCBM11).
Solution Structure, Dynamics and Binding Studies of a Family 11 Carbohydrate-Binding Module from Clostridium thermocellum (CtCBM11).
Related Articles Solution Structure, Dynamics and Binding Studies of a Family 11 Carbohydrate-Binding Module from Clostridium thermocellum (CtCBM11).
Biochem J. 2013 Jan 29;
Authors: Viegas A, Sardinha J, Freire F, Duarte DF, Carvalho AL, Fontes CM, Romão MJ, Macedo AL, Cabrita EJ
Abstract
Non-catalytic cellulosomal carbohydrate-binding modules (CBMs) are responsible for increasing the catalytic efficiency of...
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Proteins. 2011 Oct;79(10):2988-91
Authors: Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT
Abstract
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri,...
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NMR Structure and Calcium-Binding Properties of the Tellurite Resistance Protein TerD from Klebsiella pneumoniae.
NMR Structure and Calcium-Binding Properties of the Tellurite Resistance Protein TerD from Klebsiella pneumoniae.
NMR Structure and Calcium-Binding Properties of the Tellurite Resistance Protein TerD from Klebsiella pneumoniae.
J Mol Biol. 2010 Nov 25;
Authors: Pan YR, Lou YC, Seven AB, Rizo J, Chen C
The tellurium oxyanion, TeO(3)(2-), has been used in the treatment of infectious diseases caused by mycobacteria. However, many pathogenic bacteria show tellurite resistance. Several tellurite resistance genes have been identified, and these genes...
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11-30-2010 08:14 PM
[NMR paper] NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein
NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Related Articles NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Biochemistry. 2004 Feb 24;43(7):1854-61
Authors: Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H
We have recently found that a peptide from the mdm-2 binding domain of the p53 protein induced rapid membranolytic necrosis of a variety of different human...
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11-24-2010 09:25 PM
[NMR paper] NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin
NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
Related Articles NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Jan 14;275(2):1089-94
Authors: Huang W, Dolmer K, Liao X, Gettins PG
Human alpha(2)-macroglobulin-proteinase complexes bind to their receptor, the low density lipoprotein receptor-related protein (LRP), through a discrete 138-residue C-terminal receptor binding domain (RBD), which also binds to the beta-amyloid peptide. We have used NMR...
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11-18-2010 09:15 PM
[NMR paper] NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain:
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Related Articles NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Biochemistry. 1998 Jun 2;37(22):7929-40
Authors: Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER
The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision...
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11-17-2010 11:06 PM
[NMR paper] Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spec
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
EMBO J. 1994 Sep 1;13(17):3936-44
Authors: Fogh RH, Ottleben G, Rüterjans H, Schnarr M, Boelens R, Kaptein R
The structure of the 84 residue DNA binding domain of the Escherichia coli LexA repressor has been determined from...
Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.
Linear Mode
