sib1 – copy (22) – copy
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Here we used FK506-binding protein 22, a cold shock protein from the psychrophilic bacterium Shewanella sp. SIB1 (SIB1 FKBP22) as a model protein to decipher the involvement of PPIases in cold adaptation. SIB1 FKBP22 is homodimer that assumes a V-shaped structure based on a tertiary model. |
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FK506-binding protein 22 (FKBP22) from the psychrotophic bacterium Shewanella sp. SIB1 (SIB1 FKBP22) is a homodimeric protein with peptidyl prolyl cis-trans isomerase (PPIase) activity. |
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10/1/2011 · FK506‐binding protein 22 (FKBP22) from the psychrotophic bacterium Shewanella sp. SIB1 (SIB1 FKBP22) is a homodimeric protein with peptidyl prolyl cis‐trans isomerase (PPIase) activity. Each monomer consists of the N‐terminal domain responsible for dimerization and C‐terminal catalytic domain. To reveal interactions at the dimer interface of SIB1 FKBP22, the crystal structure of the N … |
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Protein Science, the flagship journal of The Protein Society, serves an international forum for publishing original reports on all scientific aspects of protein molecules. The Journal publishes papers by leading scientists from all over the world that report on advances in the understanding of proteins in the broadest sense. Protein Science aims to unify this field by cutting across … |
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FK506-binding protein 22 (FKBP22) from the psychrotrophic bacterium Shewanella sp. SIB1 is a homodimeric protein with peptidyl prolyl cis–trans isomerase (PPIase) (EC 5.2.1.8) activity. |
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SIB1 is broadcasted in subframe # 5 in the SFN for which SFN mod 8 = 0. While the repeated copies are sent in subframe # 5 for which SFN mod 2 = 0 . Thus the new copy of SIB1 is … |
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However, sib1-1 (SALK_063337) and sib1-2 (SALK_127478) mutants contain a T-DNA insertion just upstream of the stop codon and in the upstream promoter region of SIB1, respectively. RNA gel blot analysis detected low levels of SIB1 transcripts in the mutants ( Xie et al., 2010 ), indicating that the mutants are leaky. |
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