The N-Terminal Domain of Human Topoisomerase IIα Is a DNA-Dependent ATPase†

Biochemistry ◽  
1998 ◽  
Vol 37 (48) ◽  
pp. 16997-17004 ◽  
Author(s):  
Laurence P. Gardiner ◽  
David I. Roper ◽  
Timothy R. Hammonds ◽  
Anthony Maxwell
Keyword(s):  
Topoisomerase Iiα ◽  
Terminal Domain ◽  
Dependent Atpase

Structural insights into the transient closed conformation and pH dependent ATPase activity of S.Typhi GyraseB N- terminal domain

2021 ◽  
Vol 701 ◽  
pp. 108786
Author(s):  
Deepali Gupta ◽  
Pragya Tiwari ◽  
Md Anzarul Haque ◽  
Ekta Sachdeva ◽  
Md Imtaiyaz Hassan ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Closed Conformation ◽  
Terminal Domain ◽  
Dependent Atpase ◽  
Ph Dependent ◽  
Structural Insights

scholarly journals Exploration of the Role of the C-Terminal Domain of Human DNA Topoisomerase IIα in Catalytic Activity

ACS Omega ◽  
2021 ◽  
Vol 6 (40) ◽  
pp. 25892-25903
Author(s):  
Ashley C. Dougherty ◽  
Mariam G. Hawaz ◽  
Kristine G. Hoang ◽  
Judy Trac ◽  
Jacob M. Keck ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Topoisomerase Iiα ◽  
Dna Topoisomerase ◽  
Terminal Domain ◽  
Human Dna ◽  
Dna Topoisomerase Iiα

scholarly journals Bimodal Recognition of DNA Geometry by Human Topoisomerase IIα: Preferential Relaxation of Positively Supercoiled DNA Requires Elements in the C-Terminal Domain†

Biochemistry ◽  
2008 ◽  
Vol 47 (50) ◽  
pp. 13169-13178 ◽  
Author(s):  
A. Kathleen McClendon ◽  
Amanda C. Gentry ◽  
Jennifer S. Dickey ◽  
Marie Brinch ◽  
Simon Bendsen ◽  
...  
Keyword(s):  
Topoisomerase Iiα ◽  
Supercoiled Dna ◽  
Terminal Domain ◽  
Dna Geometry

scholarly journals SUMOylation of the C-terminal domain of DNA topoisomerase IIα regulates the centromeric localization of Claspin

Cell Cycle ◽  
2015 ◽  
Vol 14 (17) ◽  
pp. 2777-2784 ◽  
Author(s):  
Hyunju Ryu ◽  
Makoto M Yoshida ◽  
Vinidhra Sridharan ◽  
Akiko Kumagai ◽  
William G Dunphy ◽  
...  
Keyword(s):  
Topoisomerase Iiα ◽  
Dna Topoisomerase ◽  
Terminal Domain ◽  
Dna Topoisomerase Iiα

Structure of clathrin cages and coats in ice

1986 ◽  
Vol 44 ◽  
pp. 94-97
Author(s):  
G.P.A. Vigers ◽  
R.A. Crowther ◽  
B.M.F. Pearse
Keyword(s):  
Electron Microscopy ◽  
Heavy Chain ◽  
Outer Part ◽  
Coated Vesicles ◽  
Eukaryotic Cells ◽  
Coat Proteins ◽  
Terminal Domain ◽  
Clathrin Heavy Chain ◽  
Membrane Components

Clathrin forms the polyhedral cage of coated vesicles, which mediate the transfer of selected membrane components within eukaryotic cells. Clathrin cages and coated vesicles have been extensively studied by electron microscopy of negatively stained preparations and shadowed specimens. From these studies the gross morphology of the outer part of the polyhedral coat has been established and some features of the packing of clathrin trimers into the coat have also been described. However these previous studies have not revealed any internal details about the position of the terminal domain of the clathrin heavy chain, the location of the 100kd-50kd accessory coat proteins or the interactions of the coat with the enclosed membrane.

Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1

2019 ◽  
Vol 476 (21) ◽  
pp. 3227-3240 ◽  
Author(s):  
Shanshan Wang ◽  
Yanxiang Zhao ◽  
Long Yi ◽  
Minghe Shen ◽  
Chao Wang ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Conformational Changes ◽  
Magnaporthe Oryzae ◽  
Structural Information ◽  
Complex Structure ◽  
Critical Role ◽  
Catalytic Process ◽  
Structural Basis ◽  
Salt Bridges ◽  
Terminal Domain

Trehalose-6-phosphate (T6P) synthase (Tps1) catalyzes the formation of T6P from UDP-glucose (UDPG) (or GDPG, etc.) and glucose-6-phosphate (G6P), and structural basis of this process has not been well studied. MoTps1 (Magnaporthe oryzae Tps1) plays a critical role in carbon and nitrogen metabolism, but its structural information is unknown. Here we present the crystal structures of MoTps1 apo, binary (with UDPG) and ternary (with UDPG/G6P or UDP/T6P) complexes. MoTps1 consists of two modified Rossmann-fold domains and a catalytic center in-between. Unlike Escherichia coli OtsA (EcOtsA, the Tps1 of E. coli), MoTps1 exists as a mixture of monomer, dimer, and oligomer in solution. Inter-chain salt bridges, which are not fully conserved in EcOtsA, play primary roles in MoTps1 oligomerization. Binding of UDPG by MoTps1 C-terminal domain modifies the substrate pocket of MoTps1. In the MoTps1 ternary complex structure, UDP and T6P, the products of UDPG and G6P, are detected, and substantial conformational rearrangements of N-terminal domain, including structural reshuffling (β3–β4 loop to α0 helix) and movement of a ‘shift region' towards the catalytic centre, are observed. These conformational changes render MoTps1 to a ‘closed' state compared with its ‘open' state in apo or UDPG complex structures. By solving the EcOtsA apo structure, we confirmed that similar ligand binding induced conformational changes also exist in EcOtsA, although no structural reshuffling involved. Based on our research and previous studies, we present a model for the catalytic process of Tps1. Our research provides novel information on MoTps1, Tps1 family, and structure-based antifungal drug design.

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