Related ArticlesNMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability.
Eur J Biochem. 2000 Jan;267(2):403-13
Authors: Nicastro G, De Chiara C, Pedone E, Tatò M, Rossi M, Bartolucci S
The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx), an eubacterium growing optimally at 333 K, is the first Trx described to date from a moderate thermophilic source. To understand the molecular basis of its thermostability, the three-dimensional structure in the oxidized form was determined by NMR methods. A total of 2276 1H-NMR derived distance constraints along with 23 hydrogen-bonds, 72 phi and 27 chi1 torsion angle restraints, were used in a protocol employing simulated annealing followed by restrained molecular dynamics and restrained energy minimization. BacTrx consists of a well-defined core region of five strands of beta-sheet, surrounded by four exposed alpha-helices, features shared by other members of the thioredoxin family. The BacTrx 3D structure was compared with the Escherichia coli Trx (EcTrx) determined by X-ray crystallographic diffraction, and a number of structural differences were observed that may contribute to its thermostabilty. The results of structural analysis indicated that protein stability is due to cumulative effects, the main factor being an increased number of ionic interactions cross-linking different secondary structural elements and clamping the C-terminal alpha-helix to the core of the protein.
[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.
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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] Structure determination of the N-terminal thioredoxin-like domain of protein disulfid
Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
Biochemistry. 1996 Jun 18;35(24):7684-91
Authors: Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE
As a first step in...
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[NMR paper] Structure and dynamics of the DNA binding protein HU from Bacillus stearothermophilus
Structure and dynamics of the DNA binding protein HU from Bacillus stearothermophilus by NMR spectroscopy.
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Biopolymers. 1996;40(5):553-9
Authors: Boelens R, Vis H, Vorgias CE, Wilson KS, Kaptein R
The DNA-binding protein HU from Bacillus stearothermophilus (HUBst) is a dimer with a molecular weight of 195 kDa that is capable of bending DNA. An x-ray structure has been determined previously , but no structure could be...
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[NMR paper] Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2
Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR.
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J Biochem. 1993 Sep;114(3):421-31
Authors: Lancelin JM, Stein M, Jacquot JP
The recombinant form of the chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii that preferentially activates the NADP...
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[NMR paper] Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-di
Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional 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 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 phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy.
Protein Sci. 1992 Oct;1(10):1363-76
Authors: Wittekind...
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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...