Structural highlights
Publication Abstract from PubMed
Sequence homologs of the small MutS-related (Smr) domain, the C-terminal endonuclease domain of MutS2, also exist as stand-alone proteins. In this study, we report the crystal structure of a proteolyzed fragment of YdaL (YdaL-), a stand-alone Smr protein from Escherichia coli. In this structure, residues 86-170 assemble into a classical Smr core domain and are embraced by an N-terminal extension (residues 40-85) with an alpha/beta/alpha fold. Sequence alignment indicates that the N-terminal extension is conserved among a number of stand-alone Smr proteins, suggesting structural diversity among Smr domains. We also discovered that the DNA binding affinity and endonuclease activity of the truncated YdaL- protein were slightly lower than those of full-length YdaL-, suggesting that residues 1-38 may be involved in DNA binding.
Crystal structure of YdaL, a stand-alone small MutS-related protein from Escherichia coli.,Gui WJ, Qu QH, Chen YY, Wang M, Zhang XE, Bi LJ, Jiang T J Struct Biol. 2011 May;174(2):282-9. Epub 2011 Jan 27. PMID:21276852[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gui WJ, Qu QH, Chen YY, Wang M, Zhang XE, Bi LJ, Jiang T. Crystal structure of YdaL, a stand-alone small MutS-related protein from Escherichia coli. J Struct Biol. 2011 May;174(2):282-9. Epub 2011 Jan 27. PMID:21276852 doi:10.1016/j.jsb.2011.01.008
