3QD7

Crystal structure of YdaL, a stand-alone small MutS-related protein from Escherichia coli

3QD7 の概要

• エントリーDOI: 10.2210/pdb3qd7/pdb
• 分子名称: Uncharacterized protein ydaL (2 entities in total)
• 機能のキーワード: alpha/beta/alpha fold, endonuclease, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15442.69

構造登録者

Gui, W.J.,Qu, Q.H.,Chen, Y.Y.,Wang, M.,Zhang, X.E.,Bi, L.J.,Jiang, T. (登録日: 2011-01-18, 公開日: 2011-06-22, 最終更新日: 2024-03-20)

主引用文献

Gui, W.J.,Qu, Q.H.,Chen, Y.Y.,Wang, M.,Zhang, X.E.,Bi, L.J.,Jiang, T.
Crystal structure of YdaL, a stand-alone small MutS-related protein from Escherichia coli.
J.Struct.Biol., 174:282-289, 2011

PubMed Abstract: 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 (YdaL₃₉-₁₇₅), 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 α/β/α 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 YdaL₃₉-₁₇₅ protein were slightly lower than those of full-length YdaL₁-₁₈₇, suggesting that residues 1-38 may be involved in DNA binding.

PubMed: 21276852
DOI: 10.1016/j.jsb.2011.01.008

実験手法

X-RAY DIFFRACTION (2.3 Å)