2OJ6

Crystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain D345N mutant

2OJ6 の概要

• エントリーDOI: 10.2210/pdb2oj6/pdb
• 関連するPDBエントリー: 1KKE 2OJ5
• 分子名称: Viral attachment protein sigma 1, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: beta-barrel, beta-spiral repeat, aspartic acid cluster, greek key motif, trimer, viral protein
• 由来する生物種: Reovirus sp.
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 107568.90

構造登録者

Stehle, T.,Kirchner, E.,Dermody, T.S. (登録日: 2007-01-12, 公開日: 2007-02-13, 最終更新日: 2023-08-30)

主引用文献

Schelling, P.,Guglielmi, K.M.,Kirchner, E.,Paetzold, B.,Dermody, T.S.,Stehle, T.
The Reovirus Sigma1 Aspartic Acid Sandwich: A TRIMERIZATION MOTIF POISED FOR CONFORMATIONAL CHANGE.
J.Biol.Chem., 282:11582-11589, 2007

PubMed Abstract: Reovirus attachment protein sigma1 mediates engagement of receptors on the surface of target cells and undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway. The sigma1 protein is a filamentous, trimeric molecule with a globular beta-barrel head domain. An unusual cluster of aspartic acid residues sandwiched between hydrophobic tyrosines is located at the sigma1 subunit interface. A 1.75-A structure of the sigma1 head domain now reveals two water molecules at the subunit interface that are held strictly in position and interact with neighboring residues. Structural and biochemical analyses of mutants affecting the aspartic acid sandwich indicate that these residues and the corresponding chelated water molecules act as a plug to block the free flow of solvent and stabilize the trimer. This arrangement of residues at the sigma1 head trimer interface illustrates a new protein design motif that may confer conformational mobility during cell entry.

PubMed: 17303562
DOI: 10.1074/jbc.M610805200

実験手法

X-RAY DIFFRACTION (1.85 Å)