scholarly journals Protein Conformational Switches: From Nature to Design

2012 ◽  
Vol 18 (26) ◽  
pp. 7984-7999 ◽  
Author(s):  
Jeung-Hoi Ha ◽  
Stewart N. Loh
Keyword(s):  
Conformational Switches

The Antemortem Detection and Conformational Switches of Prion Proteins

2005 ◽  
Author(s):  
David R. Schubert ◽  
Yuanbin Liu ◽  
Roland Riek
Keyword(s):  
Prion Proteins ◽  
Conformational Switches

Coupling ligand structure to specific conformational switches in the β2-adrenoceptor

2006 ◽  
Vol 2 (8) ◽  
pp. 417-422 ◽  
Author(s):  
Xiaojie Yao ◽  
Charles Parnot ◽  
Xavier Deupi ◽  
Venkata R P Ratnala ◽  
Gayathri Swaminath ◽  
...  
Keyword(s):  
Ligand Structure ◽  
Conformational Switches

scholarly journals Resolving Conformational Switches in the Protease Ftsh using Single-Molecule FRET

2016 ◽  
Vol 110 (3) ◽  
pp. 46a
Author(s):  
Martine Ruer ◽  
Philip Gröger ◽  
Krainer Georg ◽  
Michael Schlierf
Keyword(s):  
Single Molecule ◽  
Single Molecule Fret ◽  
Conformational Switches

scholarly journals Atomic structures of the RNA end-healing 5′-OH kinase and 2′,3′-cyclic phosphodiesterase domains of fungal tRNA ligase: conformational switches in the kinase upon binding of the GTP phosphate donor

2019 ◽  
Author(s):  
Ankan Banerjee ◽  
Yehuda Goldgur ◽  
Beate Schwer ◽  
Stewart Shuman
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Fungal Pathogens ◽  
Pathogenic Fungus ◽  
Atomic Structures ◽  
Polynucleotide Kinase ◽  
Phosphate Donor ◽  
Guanine Base ◽  
Conformational Switches ◽  
Β Sheet

Abstract Fungal tRNA ligase (Trl1) rectifies RNA breaks with 2′,3′-cyclic-PO4 and 5′-OH termini. Trl1 consists of three catalytic modules: an N-terminal ligase (LIG) domain; a central polynucleotide kinase (KIN) domain; and a C-terminal cyclic phosphodiesterase (CPD) domain. Trl1 enzymes found in all human fungal pathogens are untapped targets for antifungal drug discovery. Here we report a 1.9 Å crystal structure of Trl1 KIN-CPD from the pathogenic fungus Candida albicans, which adopts an extended conformation in which separate KIN and CPD domains are connected by an unstructured linker. CPD belongs to the 2H phosphotransferase superfamily by dint of its conserved central concave β sheet and interactions of its dual HxT motif histidines and threonines with phosphate in the active site. Additional active site motifs conserved among the fungal CPD clade of 2H enzymes are identified. We present structures of the Candida Trl1 KIN domain at 1.5 to 2.0 Å resolution—as apoenzyme and in complexes with GTP•Mg2+, IDP•PO4, and dGDP•PO4—that highlight conformational switches in the G-loop (which recognizes the guanine base) and lid-loop (poised over the nucleotide phosphates) that accompany nucleotide binding.

scholarly journals A General Method to Design Allosteric Conformational Switches

2019 ◽  
Vol 116 (3) ◽  
pp. 164a
Author(s):  
Ronald L. Koder ◽  
Peter J. Schnatz ◽  
Joseph Brisendine ◽  
Craig Liang ◽  
Bernard H. Everson ◽  
...  
Keyword(s):  
Conformational Switches ◽  
General Method
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