Structural highlights
Function
A0R1C4_MYCS2
Publication Abstract from PubMed
All mycobacteria with sequenced genomes, except M. leprae, have a second Single Stranded DNA Binding protein (SSBb) in addition to the canonical one (SSBa). This paralogue from M. smegmatis (MsSSBb) has been cloned, expressed and purified. The protein, which is probably involved in stress response, has been crystallized and X-ray analyzed in the first structure elucidation of a mycobacterial SSBb. In spite of the low sequence identity between SSBas and SSBbs in mycobacteria, the tertiary and quaternary structure of the DNA binding domain of MsSSBb is similar to that observed in mycobacterial SSBas. In particular, the quaternary structure is 'clamped' using a C-terminal stretch of the N-domain, which endows the tetrameric molecule with additional stability and its characteristic shape. Comparison involving available, rather limited, structural data on SSBbs from other sources, appears to suggest that SSBbs could exhibit higher structural variability than SSBas do.
Structure of the second Single Stranded DNA Binding protein (SSBb) from Mycobacterium smegmatis.,Singh A, Varshney U, Vijayan M J Struct Biol. 2016 Sep 19. pii: S1047-8477(16)30201-5. doi:, 10.1016/j.jsb.2016.09.012. PMID:27659385[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Singh A, Varshney U, Vijayan M. Structure of the second Single Stranded DNA Binding protein (SSBb) from Mycobacterium smegmatis. J Struct Biol. 2016 Sep 19. pii: S1047-8477(16)30201-5. doi:, 10.1016/j.jsb.2016.09.012. PMID:27659385 doi:http://dx.doi.org/10.1016/j.jsb.2016.09.012