4W8C

Crystal structure of the helical domain deleted form MsrA from Clostridium oremlandii

4W8C の概要

• エントリーDOI: 10.2210/pdb4w8c/pdb
• 関連するPDBエントリー: 4LWJ
• 分子名称: Peptide methionine sulfoxide reductase MsrA, GLYCINE (3 entities in total)
• 機能のキーワード: msra, clostridium oremlandii, truncated form, oxidoreductase
• 由来する生物種: Alkaliphilus oremlandii OhILAs
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33156.68

構造登録者

Lee, E.H.,Hwang, K.Y.,Kim, H.-Y. (登録日: 2014-08-23, 公開日: 2015-07-15, 最終更新日: 2023-11-08)

主引用文献

Lee, E.H.,Lee, K.,Hwang, K.Y.,Kim, H.-Y.
Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii
Plos One, 10:e0117836-e0117836, 2015

PubMed Abstract: We previously determined the crystal structures of 1-Cys type selenoprotein MsrA from Clostridium oremlandii (CoMsrA). The overall structure of CoMsrA is unusual, consisting of two domains, the N-terminal catalytic domain and the C-terminal distinct helical domain which is absent from other known MsrA structures. Deletion of the helical domain almost completely abolishes the catalytic activity of CoMsrA. In this study, we determined the crystal structure of the helical domain-deleted (ΔH-domain) form of CoMsrA at a resolution of 1.76 Å. The monomer structure is composed of the central rolled mixed β-sheet surrounded by α-helices. However, there are significant conformational changes in the N- and C-termini and loop regions of the ΔH-domain protein relative to the catalytic domain structure of full-length CoMsrA. The active site structure in the ΔH-domain protein completely collapses, thereby causing loss of catalytic activity of the protein. Interestingly, dimer structures are observed in the crystal formed by N-terminus swapping between two molecules. The ΔH-domain protein primarily exists as a dimer in solution, whereas the full-length CoMsrA exists as a monomer. Collectively, this study provides insight into the structural basis of the essential role of the helical domain of CoMsrA in its catalysis.

PubMed: 25692691
DOI: 10.1371/journal.pone.0117836

実験手法

X-RAY DIFFRACTION (1.7568 Å)