2EXD

The solution structure of the C-terminal domain of a nfeD homolog from Pyrococcus horikoshii

2EXD の概要

• エントリーDOI: 10.2210/pdb2exd/pdb
• NMR情報: BMRB: 10118
• 分子名称: nfeD short homolog (1 entity in total)
• 機能のキーワード: nfed, membrane protein
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9203.57

構造登録者

Kuwahara, Y.,Ohno, A.,Morii, T.,Tochio, H.,Shirakawa, M.,Hiroaki, H. (登録日: 2005-11-08, 公開日: 2006-12-12, 最終更新日: 2024-05-01)

主引用文献

Kuwahara, Y.,Ohno, A.,Morii, T.,Yokoyama, H.,Matsui, I.,Tochio, H.,Shirakawa, M.,Hiroaki, H.
The solution structure of the C-terminal domain of NfeD reveals a novel membrane-anchored OB-fold.
Protein Sci., 17:1915-1924, 2008

PubMed Abstract: Nodulation formation efficiency D (NfeD) is a member of a class of membrane-anchored ClpP-class proteases. There is a second class of NfeD homologs that lack the ClpP domain. The genes of both NfeD classes usually are part of an operon that also contains a gene for a prokaryotic homolog of stomatin. (Stomatin is a major integral-membrane protein of mammalian erythrocytes.) Such NfeD/stomatin homolog gene pairs are present in more than 290 bacterial and archaeal genomes, and their protein products may be part of the machinery used for quality control of membrane proteins. Herein, we report the structure of the isolated C-terminal domain of PH0471, a Pyrococcus horikoshii NfeD homolog, which lacks the ClpP domain. This C-terminal domain (termed NfeDC) contains a five-strand beta-barrel, which is structurally very similar to the OB-fold (oligosaccharide/oligonucleotide-binding fold) domain. However, there is little sequence similarity between it and previously characterized OB-fold domains. The NfeDC domain lacks the conserved surface residues that are necessary for the binding of an OB-fold domain to DNA/RNA, an ion. Instead, its surface is composed of residues that are uniquely conserved in NfeD homologs and that form the structurally conserved surface turns and beta-bulges. There is also a conserved tryptophan present on the surface. We propose that, in general, NfeDC domains may interact with other spatially proximal membrane proteins and thereby regulate their activities.

PubMed: 18687870
DOI: 10.1110/ps.034736.108

実験手法

SOLUTION NMR