2NX7

Structure of NOWA cysteine rich domain 8

2NX7 の概要

• エントリーDOI: 10.2210/pdb2nx7/pdb
• 関連するPDBエントリー: 2HM3 2NX6
• NMR情報: BMRB: 15104
• 分子名称: Nematocyst outer wall antigen (1 entity in total)
• 機能のキーワード: cysteine rich, disulfide bonds, rich in turns, structural protein
• 由来する生物種: Hydra vulgaris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2757.18

構造登録者

Meier, S.,Jensen, P.R.,Adamczyk, P.,Bachinger, H.P.,Holstein, T.W.,Engel, J.,Ozbek, S.,Grzesiek, S. (登録日: 2006-11-17, 公開日: 2007-10-02, 最終更新日: 2024-10-30)

主引用文献

Meier, S.,Jensen, P.R.,Adamczyk, P.,Bachinger, H.P.,Holstein, T.W.,Engel, J.,Ozbek, S.,Grzesiek, S.
Sequence-structure and structure-function analysis in cysteine-rich domains forming the ultrastable nematocyst wall.
J.Mol.Biol., 368:718-728, 2007

PubMed Abstract: The nematocyst wall of cnidarians is a unique biomaterial that withstands extreme osmotic pressures, allowing an ultrafast discharge of the nematocyst capsules. Assembly of the highly robust nematocyst wall is achieved by covalent linkage of cysteine-rich domains (CRDs) from two main protein components, minicollagens and nematocyst outer wall antigen (NOWA). The bipolar minicollagens have different disulfide patterns and topologies in their N and C-terminal CRDs. The functional significance of this polarity has been elusive. Here, we show by NMR structural analysis that all representative cysteine-rich domains of NOWA are structurally related to N-terminal minicollagen domains. Natural sequence insertions in NOWA CRDs have very little effect on the tightly knit domain structures, nor do they preclude the efficient folding to a single native conformation. The different folds in NOWA CRDs and the atypical C-terminal minicollagen domain on the other hand can be directly related to different conformational preferences in the reduced states. Ultrastructural analysis in conjunction with aggregation studies argues for an association between the similar NOWA and N-terminal minicollagen domains in early stages of the nematocyst wall assembly, which is followed by the controlled association between the unusual structures of C-terminal minicollagen domains.

PubMed: 17362991
DOI: 10.1016/j.jmb.2007.02.026

実験手法

SOLUTION NMR