Solution structure and DNA binding of the catalytic domain of the large serine resolvase TnpX

2015 ◽  
Vol 28 (5) ◽  
pp. 316-324 ◽  
Author(s):  
Stephen J. Headey ◽  
Andrew Sivakumaran ◽  
Vicki Adams ◽  
Dena Lyras ◽  
Julian I. Rood ◽  
...  
Keyword(s):  
Dna Binding ◽  
Solution Structure ◽  
Catalytic Domain

scholarly journals Crystallization of and selenomethionine phasing strategy for a SETMAR–DNA complex

2016 ◽  
Vol 72 (9) ◽  
pp. 713-719 ◽  
Author(s):  
Qiujia Chen ◽  
Millie Georgiadis
Keyword(s):  
Dna Binding ◽  
Catalytic Domain ◽  
Specific Binding ◽  
Critical Role ◽  
Binding Activity ◽  
Structural Basis ◽  
Unexpected Finding ◽  
Terminal Inverted Repeat ◽  
Dna Binding Activity ◽  
New Genes

Transposable elements have played a critical role in the creation of new genes in all higher eukaryotes, including humans. Although the chimeric fusion protein SETMAR is no longer active as a transposase, it contains both the DNA-binding domain (DBD) and catalytic domain of theHsmar1transposase. The amino-acid sequence of the DBD has been virtually unchanged in 50 million years and, as a consequence, SETMAR retains its sequence-specific binding to the ancestralHsmar1terminal inverted repeat (TIR) sequence. Thus, the DNA-binding activity of SETMAR is likely to have an important biological function. To determine the structural basis for the recognition of TIR DNA by SETMAR, the design of TIR-containing oligonucleotides and SETMAR DBD variants, crystallization of DBD–DNA complexes, phasing strategies and initial phasing experiments are reported here. An unexpected finding was that oligonucleotides containing two BrdUs in place of thymidines produced better quality crystals in complex with SETMAR than their natural counterparts.

Letter to Editor: Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional regulator with a dimeric β-barrel fold

2004 ◽  
Vol 30 (2) ◽  
pp. 211-214 ◽  
Author(s):  
Alejandro D. Nadra ◽  
Tommaso Eliseo ◽  
Yu-Keung Mok ◽  
Fabio C.L. Almeida ◽  
Mark Bycroft ◽  
...  
Keyword(s):  
Dna Binding ◽  
Solution Structure ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Hpv 16

scholarly journals Solution Structure of the DNA-Binding Domain of the Tomato Heat-Stress Transcription Factor HSF24

1996 ◽  
Vol 236 (3) ◽  
pp. 911-921 ◽  
Author(s):  
Jurgen Schultheiss ◽  
Olaf Kunert ◽  
Uwe Gase ◽  
Klaus-Dieter Scharf ◽  
Lutz Nover ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Dna Binding ◽  
Solution Structure ◽  
Binding Domain ◽  
Dna Binding Domain

Solution structure of the Kluyveromyces lactis LAC9 Cd2Cys6 DNA-binding domain

1995 ◽  
Vol 2 (10) ◽  
pp. 898-905 ◽  
Author(s):  
Kevin H. Gardner ◽  
Stephen F. Anderson ◽  
Joseph E. Coleman
Keyword(s):  
Dna Binding ◽  
Solution Structure ◽  
Kluyveromyces Lactis ◽  
Binding Domain ◽  
Dna Binding Domain

scholarly journals Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor

1995 ◽  
Vol 4 (12) ◽  
pp. 2487-2498 ◽  
Author(s):  
Steven R. Van Doren ◽  
Alexander V. Kurochkin ◽  
Weidong Hu ◽  
Qi-Zhuang Ye ◽  
Linda L. Johnson ◽  
...  
Keyword(s):  
Solution Structure ◽  
Catalytic Domain

scholarly journals Structural basis of DNA replication origin recognition by human Orc6 protein binding with DNA

2020 ◽  
Vol 48 (19) ◽  
pp. 11146-11161
Author(s):  
Naining Xu ◽  
Yingying You ◽  
Changdong Liu ◽  
Maxim Balasov ◽  
Lee Tung Lun ◽  
...  
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Solution Structure ◽  
Origin Recognition Complex ◽  
Structural Basis ◽  
Dna Replication Origin ◽  
Dna Alterations ◽  
Replication Initiator ◽  
Binding Subunit ◽  
Origin Recognition

Abstract The six-subunit origin recognition complex (ORC), a DNA replication initiator, defines the localization of the origins of replication in eukaryotes. The Orc6 subunit is the smallest and the least conserved among ORC subunits. It is required for DNA replication and essential for viability in all species. Orc6 in metazoans carries a structural homology with transcription factor TFIIB and can bind DNA on its own. Here, we report a solution structure of the full-length human Orc6 (HsOrc6) alone and in a complex with DNA. We further showed that human Orc6 is composed of three independent domains: N-terminal, middle and C-terminal (HsOrc6-N, HsOrc6-M and HsOrc6-C). We also identified a distinct DNA-binding domain of human Orc6, named as HsOrc6-DBD. The detailed analysis of the structure revealed novel amino acid clusters important for the interaction with DNA. Alterations of these amino acids abolish DNA-binding ability of Orc6 and result in reduced levels of DNA replication. We propose that Orc6 is a DNA-binding subunit of human/metazoan ORC and may play roles in targeting, positioning and assembling the functional ORC at the origins.

Sign in / Sign up

Export Citation Format

Share Document