Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB.

Journal of molecular biology - 14 Jul 2006

Max Klaas E A, Zeeb Markus, Bienert Ralf, Balbach Jochen, Heinemann Udo

Abstract excerpt

Bacterial cold shock proteins (CSPs) are involved in cellular adaptation to cold stress. They bind to single-stranded nucleic acids with a KD value in the micro- to nanomolar range. Here we present the structure of the Bacillus subtilis CspB (Bs-CspB) in complex with hexathymidine (dT6) at a resolution of 1.78 A. Bs-CspB binds to dT6 with nanomolar affinity via an amphipathic interface on the protein surface....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacillus subtilis
Share to DNA, Single-Stranded
Share to Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Ligands

Share to Oligonucleotides

Share to Protein Structure, Secondary

Share to Thymine

Source

Identifiers

PMID: 16780871
DOI: 10.1016/j.jmb.2006.05.044

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

T-rich DNA single strands bind to a preformed site on the bacterial cold shock protein Bs-CspB.PMID 16780871Read ↗

Unusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.Semantic proximity Read ↗

Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis.Semantic proximity Read ↗

Acquisition of double-stranded DNA-binding ability in a hybrid protein between Escherichia coli CspA and the cold shock domain of human YB-1.Semantic proximity Read ↗

The mechanism of nucleic acid melting by a CspA family protein.Semantic proximity Read ↗

Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability.Semantic proximity Read ↗

Impact of C-terminal domains of paralogous single-stranded DNA binding proteins from Streptomyces coelicolor on their biophysical properties and biological functions.Semantic proximity Read ↗

Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces.Semantic proximity Read ↗

Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of Coulombic interactions.Semantic proximity Read ↗

Biophysical analysis of Thermus aquaticus single-stranded DNA binding protein.Semantic proximity Read ↗

Nucleic acid binding surface and dimer interface revealed by CRISPR-associated CasB protein structures.Semantic proximity Read ↗

Optimized variants of the cold shock protein from in vitro selection: structural basis of their high thermostability.Semantic proximity Read ↗

Electrostatic stabilization of a thermophilic cold shock protein.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.