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Autor:
Jeppe Kari, Nicolaj Cruys-Bagger, Kim Borch, Trine Holst Sørensen, Johan Pelck Olsen, Michael Skovbo Windahl, Kadri Alasepp, Peter Westh, Francieli Colussi
Publikováno v:
Journal of Biological Chemistry. 290:2444-2454
Cellobiohydrolases break down cellulose sequentially by sliding along the crystal surface with a single cellulose strand threaded through the catalytic tunnel of the enzyme. This so-called processive mechanism relies on a complex pattern of enzyme-su
Autor:
Xilin Zhao, Karl Drlica, Gan Luan, Kevin R. Marks, Hiroshi Hiasa, James M. Berger, Robert J. Kerns, Lisa M. Oppegard, Arkady Mustaev, Natalia Kurepina, Muhammad Malik
Publikováno v:
Journal of Biological Chemistry. 289:12300-12312
DNA gyrase and topoisomerase IV control bacterial DNA topology by breaking DNA, passing duplex DNA through the break, and then resealing the break. This process is subject to reversible corruption by fluoroquinolones, antibacterials that form drug-en
Publikováno v:
Journal of Biological Chemistry. 289:10445-10454
Crystal structures of short chain dehydrogenase-like L-threonine dehydrogenase from Cupriavidus necator (CnThrDH) in the apo and holo forms were determined at 2.25 and 2.5 Å, respectively. Structural comparison between the apo and holo forms reveale
Publikováno v:
Journal of Biological Chemistry. 288:35868-35876
The potato (Solanum tuberosum) disease resistance protein Rx has a modular arrangement that contains coiled-coil (CC), nucleotide-binding (NB), and leucine-rich repeat (LRR) domains and mediates resistance to potato virus X. The Rx N-terminal CC doma
Autor:
Anna Vitlin Gruber, Elias Eliopoulos, Abdussalam Azem, Trias Thireou, Dimitrios Fessas, Christina E. Drakou, Spyros E. Zographos, Kostas Iatrou, Georgia Kythreoti, Katerina E. Tsitsanou
Publikováno v:
Journal of Biological Chemistry. 288:33427-33438
Much physiological and behavioral evidence has been provided suggesting that insect odorant-binding proteins (OBPs) are indispensable for odorant recognition and thus are appealing targets for structure-based discovery and design of novel host-seekin
Autor:
Gábor Náray-Szabó, Ilona Szamosi, Éva Tichy-Rács, Anna Kiss-Szemán, László Polgár, Veronika Harmat, Dóra K. Menyhárd, Balázs Hornung, Klarissza Domokos, Zoltán Szeltner, Krisztina Rádi
Publikováno v:
Journal of Biological Chemistry. 288:17884-17894
Oligopeptidases impose a size limitation on their substrates, the mechanism of which has long been under debate. Here we present the structure of a hexameric serine protease, an oligopeptidase from Pyrococcus horikoshii (PhAAP), revealing a complex,
Autor:
Jackwee Lim, Sandip Basak, Asha Manikkoth Balakrishna, Gerhard Grüber, Malathy Sony Subramanian Manimekalai
Publikováno v:
Journal of Biological Chemistry. 288:11930-11939
Subunit F of V-ATPases is proposed to undergo structural alterations during catalysis and reversible dissociation from the V1VO complex. Recently, we determined the low resolution structure of F from Saccharomyces cerevisiae V-ATPase, showing an N-te
Publikováno v:
Journal of Biological Chemistry. 287:39327-39337
The ion-driven membrane rotors of ATP synthases consist of multiple copies of subunit c, forming a closed ring. Subunit c typically comprises two transmembrane helices, and the c ring features an ion-binding site in between each pair of adjacent subu
Autor:
Steven P. Smith, Jarrett J. Adams, Frédérick Faucher, Zongchao Jia, Mark A. Currie, Edward A. Bayer
Publikováno v:
Journal of Biological Chemistry. 287:26953-26961
Cellulosomes are multienzyme complexes responsible for efficient degradation of plant cell wall polysaccharides. The nonenzymatic scaffoldin subunit provides a platform for cellulolytic enzyme binding that enhances the overall activity of the bound e
Publikováno v:
Journal of Biological Chemistry. 287:8336-8346
Endo-β-1,4-glucanase from thermophilic Fervidobacterium nodosum Rt17-B1 (FnCel5A), a new member of glycosyl hydrolase family 5, is highly thermostable and exhibits the highest activity on carboxymethylcellulose among the reported homologues. To unde