The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum
The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum
Content Type Journal Article
DOI 10.1007/s10858-010-9399-7
Authors
Hiroyuki Kumeta, Hokkaido University Laboratory of Structural Biology, Graduate School of Pharmaceutical Sciences Kita 12 Nishi 6, Kita-ku Sapporo 060-0812 Japan
Noriko Miwa, Ajinomoto Co., Inc. Institute of Life Sciences 1-1 Suzuki-cho, Kawasaki-ku Kawasaki-shi 210-8681 Japan
Kenji Ogura, Hokkaido University Laboratory of Structural Biology, Graduate School of Pharmaceutical Sciences Kita 12 Nishi 6, Kita-ku Sapporo 060-0812 Japan
Yuko Kai, Ajinomoto Co., Inc. Institute of Life Sciences 1-1 Suzuki-cho, Kawasaki-ku Kawasaki-shi 210-8681 Japan
Toshimi Mizukoshi, Ajinomoto Co., Inc. Institute of Life Sciences 1-1 Suzuki-cho, Kawasaki-ku Kawasaki-shi 210-8681 Japan
Nobuhisa Shimba, Ajinomoto Co., Inc. Institute of Life Sciences 1-1 Suzuki-cho, Kawasaki-ku Kawasaki-shi 210-8681 Japan
Ei-ichiro Suzuki, Ajinomoto Co., Inc. Institute of Life Sciences 1-1 Suzuki-cho, Kawasaki-ku Kawasaki-shi 210-8681 Japan
Fuyuhiko Inagaki, Hokkaido University Laboratory of Structural Biology, Graduate School of Pharmaceutical Sciences Kita 12 Nishi 6, Kita-ku Sapporo 060-0812 Japan
NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.
NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.
NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554.
Protein Sci. 2011 Apr 21;
Authors: Atia-Tul-Wahab , Serrano P, Geralt M, Wüthrich K
The solution structure of the hypothetical phage-related protein NP_888769.1 from the gram-negative bacterium Bordetella bronchoseptica contains a well-structured core comprising a five-stranded, antiparallel ?-sheet packed...
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04-27-2011 04:03 PM
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Angew Chem Int Ed Engl. 2011 Mar 18;
Authors: Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M
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Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
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Structure. 2010 Dec 8;18(12):1678-1687
Authors: Masica DL, Ash JT, Ndao M, Drobny GP, Gray JJ
Protein-biomineral interactions are paramount to materials production in biology, including the mineral phase of hard tissue. Unfortunately, the...
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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.
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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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11-24-2010 11:14 PM
[NMR paper] Structure prediction of protein complexes by an NMR-based protein docking algorithm.
Structure prediction of protein complexes by an NMR-based protein docking algorithm.
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J Biomol NMR. 2001 May;20(1):15-21
Authors: Kohlbache O, Burchardt A, Moll A, Hildebrandt A, Bayer P, Lenhof HP
Protein docking algorithms can be used to study the driving forces and reaction mechanisms of docking processes. They are also able to speed up the lengthy process of experimental structure elucidation of protein complexes by proposing potential...
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11-19-2010 08:32 PM
[NMR paper] How do the x-ray structure and the NMR structure of FMN-binding protein differ?
How do the x-ray structure and the NMR structure of FMN-binding protein differ?
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Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):368-71
Authors: Suto K, Kawagoe K, Shibata N, Morimoto Y, Higuchi Y, Kitamura M, Nakaya T, Yasuoka N
The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio vulgaris Miyazaki F was solved by the multiple isomorphous replacement method and refined to an R factor of 15.1% at 1.3 A resolution. FMN-bp...
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11-18-2010 09:15 PM
NMR structure of the protein NP_247299.1: comparison with the crystal structure.
NMR structure of the protein NP_247299.1: comparison with the crystal structure.
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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1367-80
Authors: Jaudzems K, Geralt M, Serrano P, Mohanty B, Horst R, Pedrini B, Elsliger MA, Wilson IA, Wüthrich K
The NMR structure of the protein NP_247299.1 in solution at 313 K has been determined and is compared with the X-ray crystal structure, which was also solved in the Joint Center for...
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[NMR paper] NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
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Biochemistry. 1997 Sep 2;36(35):10709-17
Authors: Xu RX, Pawelczyk T, Xia TH, Brown SC
Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich...