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2WQT

Dodecahedral assembly of MhpD

2WQT の概要
エントリーDOI10.2210/pdb2wqt/pdb
関連するPDBエントリー1SV6
分子名称2-KETO-4-PENTENOATE HYDRATASE, PHOSPHATE ION, SODIUM ION, ... (5 entities in total)
機能のキーワードlyase, hydratase, dodecahedral form, aromatic hydrocarbons catabolism
由来する生物種ESCHERICHIA COLI
タンパク質・核酸の鎖数20
化学式量合計585510.38
構造登録者
Montgomery, M.G.,Wood, S.P. (登録日: 2009-08-27, 公開日: 2010-01-19, 最終更新日: 2023-12-20)
主引用文献Montgomery, M.G.,Coker, A.R.,Taylor, I.A.,Wood, S.P.
Assembly of a 20Nm Protein Cage by Escherichia Coli 2-Hydroxypentadienoic Acid Hydratase (Mhpd).
J.Mol.Biol., 396:1379-, 2010
Cited by
PubMed Abstract: The pentameric Escherichia coli enzyme 2-hydroxypentadienoic acid hydratase assembles to form a 20-nm-diameter particle comprising 60 protein subunits, arranged with 532 symmetry when crystallised at low pH in the presence of phosphate or sulphate ions. The particles form rapidly and are stable in solution during gel filtration at low pH. They are probably formed through trimers of pentamers, which are stabilised by the interaction of two phosphate ions with residues of the N-terminal domains of subunits at the 3-fold axis. Once the particles are formed at high concentrations of phosphate (or sulphate), they remain stable in solution at 20-fold lower concentrations of the anion. Guest molecules can be trapped within the hollow protein shell during assembly. The C-termini of the subunits are freely accessible on the surface of the protein cage and thus are ideal sites for addition of affinity tags or other modifications. These particles offer a convenient model system for studying the assembly of large symmetrical structures and a novel protein nanoparticle for encapsulation and cargo delivery.
PubMed: 20053352
DOI: 10.1016/J.JMB.2009.12.056
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.8 Å)
構造検証レポート
Validation report summary of 2wqt
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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