Related ArticlesSolution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy.
Protein Sci. 1992 Oct;1(10):1363-76
Authors: Wittekind M, Rajagopal P, Branchini BR, Reizer J, Saier MH, Klevit RE
The solution structure of the phosphocarrier protein, HPr, from Bacillus subtilis has been determined by analysis of two-dimensional (2D) NMR spectra acquired for the unphosphorylated form of the protein. Inverse-detected 2D (1H-15N) heteronuclear multiple quantum correlation nuclear Overhauser effect (HMQC NOESY) and homonuclear Hartmann-Hahn (HOHAHA) spectra utilizing 15N assignments (reported here) as well as previously published 1H assignments were used to identify cross-peaks that are not resolved in 2D homonuclear 1H spectra. Distance constraints derived from NOESY cross-peaks, hydrogen-bonding patterns derived from 1H-2H exchange experiments, and dihedral angle constraints derived from analysis of coupling constants were used for structure calculations using the variable target function algorithm, DIANA. The calculated models were refined by dynamical simulated annealing using the program X-PLOR. The resulting family of structures has a mean backbone rmsd of 0.63 A (N, C alpha, C', O atoms), excluding the segments containing residues 45-59 and 84-88. The structure is comprised of a four-stranded antiparallel beta-sheet with two antiparallel alpha-helices on one side of the sheet. The active-site His 15 residue serves as the N-cap of alpha-helix A, with its N delta 1 atom pointed toward the solvent to accept the phosphoryl group during the phosphotransfer reaction with enzyme I. The existence of a hydrogen bond between the side-chain oxygen atom of Tyr 37 and the amide proton of Ala 56 is suggested, which may account for the observed stabilization of the region that includes the beta-turn comprised of residues 37-40. If the beta alpha beta beta alpha beta (alpha) folding topology of HPr is considered with the peptide chain polarity reversed, the protein fold is identical to that described for another group of beta alpha beta beta alpha beta proteins that include acylphosphatase and the RNA-binding domains of the U1 snRNP A and hnRNP C proteins.
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] Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.
Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.
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Biochem Biophys Res Commun. 2005 Sep 23;335(2):361-6
Authors: Hastings AF, Otting G, Folmer RH, Duggin IG, Wake RG, Wilce MC, Wilce JA
Termination of DNA replication in Bacillus subtilis involves the polar arrest of replication forks by a specific complex formed between the dimeric 29 kDa replication terminator...
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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.
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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] Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectrosc
Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy.
Related Articles Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy.
Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):421-4
Authors: Vivian JP, Wilce JA, Hastings AF, Wilce MC
The replication terminator protein (RTP)-DNA complex of Bacillus subtilis is responsible for the arrest of DNA replication at terminator sites in the B. subtilis chromosome. The crystallization and preliminary diffraction data analysis...
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Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
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Biochemistry. 2010 Sep 15;
Authors: Chang YC, Franch WR, Oas TG
Protein folding intermediates are often imperative to overall folding processes and consequent biological functions. However, the low population and transient nature of the intermediate states often hinder the biochemical and biophysical characterization. Previous studies have demonstrated that Bacillus...
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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] Low resolution solution structure of the Bacillus subtilis glucose permease IIA domai
Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopy.
FEBS Lett. 1992 Jan 20;296(2):148-52
Authors: Fairbrother WJ, Gippert GP, Reizer J, Saier MH, Wright PE
A low resolution...