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排序方式: 共有204条查询结果,搜索用时 640 毫秒
41.
Zukang Feng John D. Westbrook Raul Sala Oliver S. Smart Gérard Bricogne Masaaki Matsubara Issaku Yamada Shinichiro Tsuchiya Kiyoko F. Aoki-Kinoshita Jeffrey C. Hoch Genji Kurisu Sameer Velankar Stephen K. Burley Jasmine Y. Young 《Structure (London, England : 1993)》2021,29(4):393-400.e1
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Helen M. Berman Paul D. Adams Alexandre A. Bonvin Stephen K. Burley Bridget Carragher Wah Chiu Frank DiMaio Thomas E. Ferrin Margaret J. Gabanyi Thomas D. Goddard Patrick R. Griffin Juergen Haas Christian A. Hanke Jeffrey C. Hoch Gerhard Hummer Genji Kurisu Catherine L. Lawson Alexander Leitner Andrej Sali 《Structure (London, England : 1993)》2019,27(12):1745-1759
46.
Almo SC Bonanno JB Sauder JM Emtage S Dilorenzo TP Malashkevich V Wasserman SR Swaminathan S Eswaramoorthy S Agarwal R Kumaran D Madegowda M Ragumani S Patskovsky Y Alvarado J Ramagopal UA Faber-Barata J Chance MR Sali A Fiser A Zhang ZY Lawrence DS Burley SK 《Journal of structural and functional genomics》2007,8(2-3):121-140
47.
Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications 总被引:1,自引:0,他引:1
Rao KN Kumaran D Seetharaman J Bonanno JB Burley SK Swaminathan S 《Protein science : a publication of the Protein Society》2006,15(7):1735-1744
We report here the crystal structure of a trehalose-6-phosphate phosphatase-related protein (T6PP) from Thermoplasma acidophilum, TA1209, determined by the dual-wavelength anomalous diffraction (DAD) method. T6PP is a member of the haloacid dehalogenase (HAD) superfamily with significant sequence homology with trehalose-6-phosphate phosphatase, phosphoserine phosphatase, P-type ATPases and other members of the family. T6PP possesses a core domain of known alpha/beta-hydrolase fold, characteristic of the HAD family, and a cap domain, with a tertiary fold consisting of a four-stranded beta-sheet with two alpha-helices on one side of the sheet. An active-site magnesium ion and a glycerol molecule bound at the interface between the two domains provide insight into the mode of substrate binding by T6PP. A trehalose-6-phosphate molecule modeled into a cage formed by the two domains makes favorable interactions with the protein molecule. We have confirmed that T6PP is a trehalose phosphatase from amino acid sequence, three-dimensional structure, and biochemical assays. 相似文献
48.
L.M. Sampaleanu M. Ayers S. Tammam S.K. Burley L.L. Burrows P.L. Howell 《Journal of molecular biology》2009,394(1):143-159
Type IV pili (T4P) are bacterial virulence factors responsible for attachment to surfaces and for twitching motility, a motion that involves a succession of pilus extension and retraction cycles. In the opportunistic pathogen Pseudomonas aeruginosa, the PilM/N/O/P proteins are essential for T4P biogenesis, and genetic and biochemical analyses strongly suggest that they form an inner-membrane complex. Here, we show through co-expression and biochemical analysis that the periplasmic domains of PilN and PilO interact to form a heterodimer. The structure of residues 69-201 of the periplasmic domain of PilO was determined to 2.2 Å resolution and reveals the presence of a homodimer in the asymmetric unit. Each monomer consists of two N-terminal coiled coils and a C-terminal ferredoxin-like domain. This structure was used to generate homology models of PilN and the PilN/O heterodimer. Our structural analysis suggests that in vivo PilN/O heterodimerization would require changes in the orientation of the first N-terminal coiled coil, which leads to two alternative models for the role of the transmembrane domains in the PilN/O interaction. Analysis of PilN/O orthologues in the type II secretion system EpsL/M revealed significant similarities in their secondary structures and the tertiary structures of PilO and EpsM, although the way these proteins interact to form inner-membrane complexes appears to be different in T4P and type II secretion. Our analysis suggests that PilN interacts directly, via its N-terminal tail, with the cytoplasmic protein PilM. This work shows a direct interaction between the periplasmic domains of PilN and PilO, with PilO playing a key role in the proper folding of PilN. Our results suggest that PilN/O heterodimers form the foundation of the inner-membrane PilM/N/O/P complex, which is critical for the assembly of a functional T4P complex. 相似文献
49.
Berman HM Burley SK Chiu W Sali A Adzhubei A Bourne PE Bryant SH Dunbrack RL Fidelis K Frank J Godzik A Henrick K Joachimiak A Heymann B Jones D Markley JL Moult J Montelione GT Orengo C Rossmann MG Rost B Saibil H Schwede T Standley DM Westbrook JD 《Structure (London, England : 1993)》2006,14(8):1211-1217
50.
Parthasarathy Sampathkumar Frances Lu Xun Zhao Zhenzhen Li Jeremiah Gilmore Kevin Bain Marc E. Rutter Tarun Gheyi Kenneth D. Schwinn Jeffrey B. Bonanno Ursula Pieper J. Eduardo Fajardo Andras Fiser Steven C. Almo Subramanyam Swaminathan Mark R. Chance David Baker Shane Atwell Devon A. Thompson J. Spencer Emtage Stephen R. Wasserman Andrej Sali J. Michael Sauder Stephen K. Burley 《Proteins》2010,78(14):3056-3062