Structure of the single-stranded DNA-binding protein SSB from Thermus aquaticus.
نویسندگان
چکیده
The crystal structure of the single-stranded DNA-binding protein from Thermus aquaticus has been solved and refined at 1.85 A resolution. Two monomers, each encompassing two oligonucleotide/oligosaccharide-binding (OB) domains and a number of flexible beta-hairpin loops, form an oligomer of approximate D(2) symmetry typical of bacterial SSBs. Comparison with other SSB structures confirms considerable variability in the mode of oligomerization and aggregation of SSB oligomers.
منابع مشابه
3D structure of Thermus aquaticus single-stranded DNA–binding protein gives insight into the functioning of SSB proteins
In contrast to the majority of tetrameric SSB proteins, the recently discovered SSB proteins from the Thermus/Deinoccus group form dimers. We solved the crystal structures of the SSB protein from Thermus aquaticus (TaqSSB) and a deletion mutant of the protein and show the structure of their ssDNA binding domains to be similar to the structure of tetrameric SSBs. Two conformations accompanied by...
متن کاملIdentification and properties of the Deinococcus grandis and Deinococcus proteolyticus single-stranded DNA binding proteins (SSB).
To study the biochemical properties of SSB's from Deinococcus grandis (DgrSSB) and Deinococcus proteolyticus (DprSSB), we have cloned the ssb genes obtained by PCR and have developed Escherichia coli overexpression systems. The genes consist of an open reading frame of 891 (DgrSSB) and 876 (DprSSB) nucleotides encoding proteins of 296 and 291 amino acids with a calculated molecular mass of 32.2...
متن کاملSingle molecule analysis of Thermus thermophilus SSB protein dynamics on single-stranded DNA
Single-stranded (ss) DNA binding (SSB) proteins play central roles in DNA replication, recombination and repair in all organisms. We previously showed that Escherichia coli (Eco) SSB, a homotetrameric bacterial SSB, undergoes not only rapid ssDNA-binding mode transitions but also one-dimensional diffusion (or migration) while remaining bound to ssDNA. Whereas the majority of bacterial SSB famil...
متن کاملCrystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage.
Single-stranded DNA (ssDNA)-binding (SSB) proteins are uniformly required to bind and protect single-stranded intermediates in DNA metabolic pathways. All bacterial and eukaryotic SSB proteins studied to date oligomerize to assemble four copies of a conserved domain, called an oligonucleotide/oligosaccharide-binding (OB) fold, that cooperate in nonspecific ssDNA binding. The vast majority of ba...
متن کاملCloning and Expression of Thermus Aquaticus DNA Polymerase Gene, Using a Thermo-Inducible Expression Vector
DNA polymerase gene from Thermus aquaticus strain YT1 was amplified using VENTTM DNA po-lymerase and cloned under the control of X.PR promoter and expression was induced by a shift in tern perature. The culture was then sonicated, and after centrifugation the lysate was treated with polyethyleneimine followed by a salting-out step. Finally the protein was precipitated with ammonium sulfate and...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Acta crystallographica. Section D, Biological crystallography
دوره 62 Pt 11 شماره
صفحات -
تاریخ انتشار 2006