scholarly journals The crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acids

2014 ◽  
Vol 42 (7) ◽  
pp. 4712-4722 ◽  
Author(s):  
P.-H. Kuo ◽  
C.-H. Chiang ◽  
Y.-T. Wang ◽  
L. G. Doudeva ◽  
H. S. Yuan
Keyword(s):  
Crystal Structure ◽  
Nucleic Acids ◽  
Specific Recognition ◽  
Dna Complex

Crystal Structure of a bZIP/DNA Complex at 2.2 Å: Determinants of DNA Specific Recognition

1995 ◽  
Vol 254 (4) ◽  
pp. 657-667 ◽  
Author(s):  
Walter Keller ◽  
Peter König ◽  
Timothy J. Richmond
Keyword(s):  
Crystal Structure ◽  
Specific Recognition ◽  
Dna Complex

Helicase mechanisms and the coupling of helicases within macromolecular machines Part I: Structures and properties of isolated helicases

2002 ◽  
Vol 35 (4) ◽  
pp. 431-478 ◽  
Author(s):  
Emmanuelle Delagoutte ◽  
Peter H. von Hippel
Keyword(s):  
Crystal Structure ◽  
Nucleic Acid ◽  
Nucleic Acids ◽  
Binding Site ◽  
Crystal Structures ◽  
Base Pair ◽  
Biochemical Properties ◽  
Functional Coupling ◽  
Hexameric Helicases ◽  
Base Pair Opening

1. Mechanisms of nucleic acid (NA) unwinding by helicases 4322. Helicases may take advantage of ‘breathing’ fluctuations in dsNAs 4342.1 Stability and dynamics of dsNAs 4342.2 dsNAs ‘breathe’ in isolation 4352.3 Thermodynamics of terminal base pairs of dsNA 4382.4 Thermal fluctuations may be responsible for sequential base-pair opening at replication forks 4392.5 Helicases may capture single base-pair opening events sequentially 4403. Biochemical properties of helicases 4433.1 Binding of NAs 4433.2 Binding and hydrolysis of NTP 4453.3 Coordination between NA binding and NTP binding and hydrolysis activities 4464. Helicase structures and mechanistic consequences 4474.1 Amino-acid sequence analysis reveals conserved motifs that constitute the NTP-binding pocket and a portion of the NA-binding site 4474.2 Organization of hepatitis virus C NS3 RNA helicase 4494.2.1 Biochemical properties of HCV NS3 4494.2.2 Crystal structures of HCV NS3 helicase 4504.2.2.1 The apoprotein 4504.2.2.2 The protein–dU8 complex 4504.2.3 A possible unwinding mechanism 4524.2.4 What is the functional oligomeric state of HCV NS3? 4524.3 Organization of the PcrA helicase 4534.3.1 The apoenzyme and ADP–PcrA complex 4544.3.2 The protein–DNA–sulfate complex 4564.3.3 The PcrA–DNA–ADPNP complex 4564.3.4 A closer look at the NTP-binding site in the crystal structure of PcrA–ADPNP–DNA 4574.3.5 Communication between domains A and B 4574.3.6 How might ssDNA stimulate the ATPase activity of PcrA? 4574.3.7 A possible helicase translocation mechanism 4584.3.8 A possible unwinding mechanism 4584.4 Organization of the Rep helicase 4594.4.1 Biochemical properties 4594.4.2 Crystal structure of Rep bound to ssDNA 4624.5 Organization of the RecG helicase 4624.6 Hexameric helicases 4664.6.1 Insights from crystal structures of hexameric helicases 4674.6.2 Possible translocation and unwinding mechanisms 4685. Conclusions 4696. Acknowledgments 4727. References 472Helicases are proteins that harness the chemical free energy of ATP hydrolysis to catalyze the unwinding of double-stranded nucleic acids. These enzymes have been much studied in isolation, and here we review what is known about the mechanisms of the unwinding process. We begin by considering the thermally driven ‘breathing’ of double-stranded nucleic acids by themselves, in order to ask whether helicases might take advantage of some of these breathing modes. We next provide a brief summary of helicase mechanisms that have been elucidated by biochemical, thermodynamic, and kinetic studies, and then review in detail recent structural studies of helicases in isolation, in order to correlate structural findings with biophysical and biochemical results. We conclude that there are certainly common mechanistic themes for helicase function, but that different helicases have devised solutions to the nucleic acid unwinding problem that differ in structural detail. In Part II of this review (to be published in the next issue of this journal) we consider how these mechanisms are further modified to reflect the functional coupling of these proteins into macromolecular machines, and discuss the role of helicases in several central biological processes to illustrate how this coupling actually works in the various processes of gene expression.

scholarly journals The crystal structure of an intact human Max–DNA complex: new insights into mechanisms of transcriptional control

Structure ◽  
1997 ◽  
Vol 5 (4) ◽  
pp. 509-520 ◽  
Author(s):  
P Brownlie ◽  
TA Ceska ◽  
M Lamers ◽  
C Romier ◽  
G Stier ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Transcriptional Control ◽  
Dna Complex

Analysis of the 2.0 Å Crystal Structure of the Protein−DNA Complex of the Human PDEF Ets Domain Bound to the Prostate Specific Antigen Regulatory Site†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (19) ◽  
pp. 7095-7106 ◽  
Author(s):  
Yangzhou Wang ◽  
Lin Feng ◽  
Meriem Said ◽  
Sophia Balderman ◽  
Zahra Fayazi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Prostate Specific Antigen ◽  
Specific Antigen ◽  
Regulatory Site ◽  
Ets Domain ◽  
Dna Complex

scholarly journals Specific recognition of guanines in non-duplex regions of nucleic acids with potassium tungstate and hydrogen peroxide

2014 ◽  
Vol 43 (1) ◽  
pp. e3-e3 ◽  
Author(s):  
Wuxiang Mao ◽  
Xiaowei Xu ◽  
Huan He ◽  
Rong Huang ◽  
Xi Chen ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Nucleic Acids ◽  
Specific Recognition
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