Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the β1,4-galactosyltransferase-I11Edited by R. Huber

2001 ◽  
Vol 310 (1) ◽  
pp. 205-218 ◽  
Author(s):  
B Ramakrishnan ◽  
Pradman K Qasba
Keyword(s):  
Crystal Structure ◽  
Conformational Change ◽  
Lactose Synthase ◽  
Large Conformational Change

scholarly journals Crystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-Å resolution: A large conformational change in ADP-dependent glucokinase

2009 ◽  
Vol 11 (10) ◽  
pp. 2456-2463 ◽  
Author(s):  
Hideaki Tsuge ◽  
Haruhiko Sakuraba ◽  
Toru Kobe ◽  
Akira Kujime ◽  
Nobuhiko Katunuma ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Change ◽  
Pyrococcus Horikoshii ◽  
Large Conformational Change

scholarly journals Light and heat control over secondary structure and amyloid-like fiber formation in an overcrowded-alkene-modified Trp zipper

2015 ◽  
Vol 6 (12) ◽  
pp. 7311-7318 ◽  
Author(s):  
Claudia Poloni ◽  
Marc C. A. Stuart ◽  
Pieter van der Meulen ◽  
Wiktor Szymanski ◽  
Ben L. Feringa
Keyword(s):  
Secondary Structure ◽  
Conformational Change ◽  
Fiber Formation ◽  
Major Influence ◽  
Heat Control ◽  
Large Conformational Change

The use of an overcrowded alkene photoswitch to control a model β-hairpin peptide is described. The light-induced, large conformational change has major influence on the secondary structure and the aggregation of the peptide, permitting the triggered formation of amyloid-like fibrils.

Crystal Structure of the Complex of the Variable Domain of Antibody D1.3 and Turkey Egg White Lysozyme: A Novel Conformational Change in Antibody CDR-L3 Selects for Antigen

1996 ◽  
Vol 257 (5) ◽  
pp. 889-894 ◽  
Author(s):  
Bradford C. Braden ◽  
Barry A. Fields ◽  
Xavier Ysern ◽  
Fernando A. Goldbaum ◽  
William Dall'Acqua ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Conformational Change ◽  
Egg White ◽  
Variable Domain ◽  
Egg White Lysozyme

scholarly journals A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1)

2018 ◽  
Vol 29 (9) ◽  
pp. 1060-1074 ◽  
Author(s):  
Tomohiro Kubo ◽  
Yuqing Hou ◽  
Deborah A. Cochran ◽  
George B. Witman ◽  
Toshiyuki Oda
Keyword(s):  
Conformational Change ◽  
Molecular Mechanism ◽  
Wild Type ◽  
Sliding Direction ◽  
Large Conformational Change ◽  
Dynein Arms ◽  
Biochemical Analyses

Motility of cilia/flagella is generated by a coordinated activity of thousands of dyneins. Inner dynein arms (IDAs) are particularly important for the formation of ciliary/flagellar waveforms, but the molecular mechanism of IDA regulation is poorly understood. Here we show using cryoelectron tomography and biochemical analyses of Chlamydomonas flagella that a conserved protein FAP44 forms a complex that tethers IDA f (I1 dynein) head domains to the A-tubule of the axonemal outer doublet microtubule. In wild-type flagella, IDA f showed little nucleotide-dependent movement except for a tilt in the f β head perpendicular to the microtubule-sliding direction. In the absence of the tether complex, however, addition of ATP and vanadate caused a large conformational change in the IDA f head domains, suggesting that the movement of IDA f is mechanically restricted by the tether complex. Motility defects in flagella missing the tether demonstrates the importance of the IDA f-tether interaction in the regulation of ciliary/flagellar beating.

scholarly journals Crystal Structure of Dengue Virus Type 1 Envelope Protein in the Postfusion Conformation and Its Implications for Membrane Fusion

2009 ◽  
Vol 83 (9) ◽  
pp. 4338-4344 ◽  
Author(s):  
Vinod Nayak ◽  
Moshe Dessau ◽  
Kaury Kucera ◽  
Karen Anthony ◽  
Michel Ledizet ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dengue Virus ◽  
Conformational Change ◽  
Virus Type ◽  
Envelope Protein ◽  
Lipid Membrane ◽  
Ph Sensor ◽  
Endosomal Membrane ◽  
Domain Iii

ABSTRACT Dengue virus relies on a conformational change in its envelope protein, E, to fuse the viral lipid membrane with the endosomal membrane and thereby deliver the viral genome into the cytosol. We have determined the crystal structure of a soluble fragment E (sE) of dengue virus type 1 (DEN-1). The protein is in the postfusion conformation even though it was not exposed to a lipid membrane or detergent. At the domain I-domain III interface, 4 polar residues form a tight cluster that is absent in other flaviviral postfusion structures. Two of these residues, His-282 and His-317, are conserved in flaviviruses and are part of the “pH sensor” that triggers the fusogenic conformational change in E, at the reduced pH of the endosome. In the fusion loop, Phe-108 adopts a distinct conformation, forming additional trimer contacts and filling the bowl-shaped concavity observed at the tip of the DEN-2 sE trimer.

scholarly journals Crystal Structure Analysis of Extrinsic PsbP Protein of Photosystem II Reveals a Manganese-Induced Conformational Change

2015 ◽  
Vol 8 (4) ◽  
pp. 664-666 ◽  
Author(s):  
Peng Cao ◽  
Yuan Xie ◽  
Mei Li ◽  
Xiaowei Pan ◽  
Hongmei Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Photosystem Ii ◽  
Conformational Change ◽  
Structure Analysis ◽  
Crystal Structure Analysis ◽  
Psbp Protein
Sign in / Sign up

Export Citation Format

Share Document