[NMR paper] Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct ?-helical architecture and provides first structural representative of protein domain family PF14203.
Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct ?-helical architecture and provides first structural representative of protein domain family PF14203.
Related ArticlesSolution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct ?-helical architecture and provides first structural representative of protein domain family PF14203.
J Struct Funct Genomics. 2013 Sep 19;
Authors: Pulavarti SV, Eletsky A, Lee HW, Acton TB, Xiao R, Everett JK, Prestegard JH, Montelione GT, Szyperski T
Abstract
A high-quality structure of the 68-residue protein CD1104B from Clostridium difficile strain 630 exhibits a distinct all ?-helical fold. The structure presented here is the first representative of bacterial protein domain family PF14203 (currently 180 members) of unknown function (DUF4319) and reveals that the side-chains of the only two strictly conserved residues (Glu 8 and Lys 48) form a salt bridge. Moreover, these two residues are located in the vicinity of the largest surface cleft which is predicted to contribute to a surface area involved in protein-protein interactions. This, along with its coding in transposon CTn4, suggests that CD1104B (and very likely all members of Pfam 14203) functions by interacting with other proteins required for the transfer of transposons between different bacterial species.
PMID: 24048810 [PubMed - as supplied by publisher]
[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).
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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...
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[NMR paper] 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.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif 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 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...
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Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
J Struct Funct Genomics. 2011 Sep 9;
Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
Abstract
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NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
J Biol Chem. 2011 May 3;
Authors: Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS
Vaccinia-related kinase 1 (VRK1) is one of the mitotic kinases which play important roles in cell cycle, nuclear condensation and transcription regulation. Kinase...
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A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
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Chemistry. 2011 Feb 1;17(5):1547-1560
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-),...
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A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
A Solution NMR Study of the Interactions of Oligomannosides and the Anti-HIV-1 2G12 Antibody Reveals Distinct Binding Modes for Branched Ligands*
Chemistry. 2011 Jan 5;
Authors: Enríquez-Navas PM, Marradi M, Padro D, Angulo J, Penadés S
The structural and affinity details of the interactions of synthetic oligomannosides, linear (di-, tri-, and tetra-) and branched (penta- and hepta-), with the broadly...
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[NMR paper] Validation of helical tilt angles in the solution NMR structure of the Z domain of St
Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data.
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Protein Sci. 2004 Feb;13(2):549-54
Authors: Zheng D, Aramini JM, Montelione GT
Staphylococcal protein A (SpA) is a virulence factor from Staphylococcus aureus that is able to bind to...
Solution NMR structure of CD1104B from pathogenic Clostridium difficile reveals a distinct ?-helical architecture and provides first structural representative of protein domain family PF14203.
Linear Mode
