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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[NMR paper] NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a
NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a plant pathogen Xanthomonas campestris pv. campestris.
Related Articles NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a plant pathogen Xanthomonas campestris pv. campestris.
J Biomol NMR. 2005 Feb;31(2):167-72
Authors: Chin KH, Lin FY, Hu YC, Sze KH, Lyu PC, Chou SH
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[NMR paper] Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc
Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
Related Articles Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
J Mol Biol. 2004 Nov 19;344(2):567-83
Authors: Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA
IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur () clusters. We report the NMR...
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NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
J Biomol NMR. 2010 Aug;47(4):283-8
Authors: Chen J, Li Q, Liu CC, Zhou B, Bu G, Wang J
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09-24-2010 03:50 AM
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
Related Articles Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis.
J Am Chem Soc. 2010 Aug 20;
Authors: Hu Y, Zhao E, Li H, Xia B, Jin C
The twin-arginine transport (Tat) system translocates folded proteins across the bacterial cytoplasmic or chloroplast thylakoid membrane of plants. The Tat system in most Gram-positive...
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08-25-2010 02:04 PM
[NMR paper] Posttranslational modification of Klebsiella pneumoniae flavodoxin by covalent attach
Posttranslational modification of Klebsiella pneumoniae flavodoxin by covalent attachment of coenzyme A, shown by 31P NMR and electrospray mass spectrometry, prevents electron transfer from the nifJ protein to nitrogenase. A possible new regulatory mechanism for biological nitrogen fixation.
Related Articles Posttranslational modification of Klebsiella pneumoniae flavodoxin by covalent attachment of coenzyme A, shown by 31P NMR and electrospray mass spectrometry, prevents electron transfer from the nifJ protein to nitrogenase. A possible new regulatory mechanism for biological...
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08-21-2010 11:41 PM
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport S
Solution NMR Structure of the TatA Component of the Twin-Arginine Protein Transport System from Gram-Positive Bacterium Bacillus subtilis
Yunfei Hu et al
http://pubs.acs.org//appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1053785/aop/images/medium/ja-2010-053785_0001.gifJournal of the American Chemical Society, Volume 0, Issue 0, Articles ASAP (As Soon As Publishable).
Source: Journal of the American Chemical Society
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08-21-2010 05:17 AM
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Content Type Journal Article
DOI 10.1007/s10858-010-9426-8
Authors
Jianglei Chen, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Qianqian Li, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Chia-Chen Liu, Washington University Departments of Pediatrics, and Cell Biology and Physiology, School of Medicine St. Louis MO 63110 USA
NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae
Linear Mode
