2VW9

Single stranded DNA binding protein complex from Helicobacter pylori

Summary for 2VW9

• Entry DOI: 10.2210/pdb2vw9/pdb
• Descriptor: SINGLE-STRANDED DNA BINDING PROTEIN, POLY-DT (3 entities in total)
• Functional Keywords: dna replication, single-stranded dna, single-stranded dna binding protein, oligonucleotide/oligosaccharide binding fold, helicobacter pylori, ob-fold, dna damage, dna repair, dna-binding protein, dna binding protein
• Biological source: HELICOBACTER PYLORI
• Total number of polymer chains: 3
• Total formula weight: 40539.54

Authors

Chan, K.-W.,Wang, C.-H.,Lee, Y.-J.,Sun, Y.-J. (deposition date: 2008-06-18, release date: 2009-06-02, Last modification date: 2023-12-13)

Primary citation

Chan, K.-W.,Lee, Y.-J.,Wang, C.-H.,Huang, H.,Sun, Y.-J.
Single-Stranded DNA-Binding Protein Complex from Helicobacter Pylori Suggests an Ssdna-Binding Surface.
J.Mol.Biol., 388:508-, 2009

PubMed Abstract: Single-stranded DNA (ssDNA)-binding protein (SSB) plays an important role in DNA replication, recombination, and repair. SSB consists of an N-terminal ssDNA-binding domain with an oligonucleotide/oligosaccharide binding fold and a flexible C-terminal tail involved in protein-protein interactions. SSB from Helicobacter pylori (HpSSB) was isolated, and the ssDNA-binding characteristics of HpSSB were analyzed by fluorescence titration and electrophoretic mobility shift assay. Tryptophan fluorescence quenching was measured as 61%, and the calculated cooperative affinity was 5.4x10(7) M(-1) with an ssDNA-binding length of 25-30 nt. The crystal structure of the C-terminally truncated protein (HpSSBc) in complex with 35-mer ssDNA [HpSSBc-(dT)(35)] was determined at a resolution of 2.3 A. The HpSSBc monomer folds as an oligonucleotide/oligosaccharide binding fold with a Y-shaped conformation. The ssDNA wrapped around the HpSSBc tetramer through a continuous binding path comprising five essential aromatic residues and a positively charged surface formed by numerous basic residues.

PubMed: 19285993
DOI: 10.1016/J.JMB.2009.03.022

Experimental method

X-RAY DIFFRACTION (2.3 Å)