[NMR paper] Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state
ATP binding cassette (ABC) proteins are present in all phyla of life and form one of the largest protein families. The Bacillus subtilis ABC transporter BmrA is a functional homodimer that can extrude many different harmful compounds out of the cell. Each BmrA monomer is composed of a transmembrane domain (TMD) and a nucleotide binding domain (NBD). While the TMDs of ABC transporters are sequentially diverse, the highly conserved NBDs harbor distinctive conserved motifs that enable nucleotide...
[NMR paper] Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.
Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.
Related Articles Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.
Biomol NMR Assign. 2013 Dec 24;
Authors: Castellen P, Sforça ML, Gueiros-Filho FJ, de Mattos Zeri AC
Abstract
Bacterial cell division proteins must assemble at the middle of the cell to ensure the viability of both daughter cells. The first step in the assembly of the...
NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633.
NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633.
NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633.
Biomol NMR Assign. 2011 Jun 5;
Authors: Christ NA, Duchardt-Ferner E, Düsterhus S, Kötter P, Entian KD, Wöhnert J
Bacillus subtilis ATCC 6633 produces the lipid II targeting lantibiotic subtilin. For self-protection these gram-positive bacteria express a cluster of four self-immunity proteins named SpaIFEG. SpaI is a 16.8*kDa lipoprotein which is attached to the...
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[NMR paper] NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
Related Articles NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
J Biomol NMR. 2005 Jul;32(3):258
Authors: Zhang X, Yu C, Xia B, Jin C
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[NMR paper] Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Related Articles Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.
Biochemistry. 2005 Aug 2;44(30):10153-63
Authors: Mishima M, Shida T, Yabuki K, Kato K, Sekiguchi J, Kojima C
Bacillus subtilis CwlC is a cell wall lytic N-acetylmuramoyl-l-alanine amidase that plays an...
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[NMR paper] High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response
High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition.
Biochemistry. 1997 Aug 19;36(33):10015-25
Authors: Feher VA, Zapf JW, Hoch JA, Whiteley JM, McIntosh LP, Rance M, Skelton NJ,...
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[NMR paper] Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as mo
Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
Eur J Biochem. 1993 Apr 15;213(2):781-8
Authors: Löw A, Sprinzl M, Limmer S
Proton-NMR signals in the downfield region (below approximately 10...
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[NMR paper] Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophil
Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR.
Related Articles Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR.
Biochemistry. 1992 Mar 24;31(11):2970-7
Authors: Limmer S, Reiser CO, Schirmer NK, Grillenbeck NW, Sprinzl M
Proton NMR experiments of the GTP/GDP-binding protein EF-Tu from the extremely thermophilic bacterium Thermus thermophilus HB8 in H2O have been performed paying special attention to the...
Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state
Linear Mode
