1TI1

crystal structure of a mutant DsbA

1TI1 の概要

• エントリーDOI: 10.2210/pdb1ti1/pdb
• 関連するPDBエントリー: 1DSB 1FVK
• 分子名称: Thiol:disulfide interchange protein dsbA, DODECANE (3 entities in total)
• 機能のキーワード: oxidoreductase, proline, thiol, detergent
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P24991
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21293.29

構造登録者

Kone, A.,Serre, L. (登録日: 2004-06-02, 公開日: 2005-05-03, 最終更新日: 2024-10-30)

主引用文献

Ondo-Mbele, E.,Vives, C.,Kone, A.,Serre, L.
Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant.
J.Mol.Biol., 347:555-563, 2005

PubMed Abstract: Escherichia coli DsbA belongs to the thioredoxin family and catalyzes the formation of disulfide bonds during the folding of proteins in the bacterial periplasm. It active site (C30-P31-H32-C33) consists of a disulfide bridge that is transferred to newly translocated proteins. The work reported here refers to the DsbA mutant termed C33A that retains, towards reduced unfolded thrombin inhibitor, an activity comparable with the wild-type enzyme. Besides, C33A is also able to form a stable covalent complex with DsbB, the membrane protein responsible for maintaining DsbA in its active form. We have determined the crystal structure of C33A at 2.0 angstroms resolution. Although the general architecture of wt DsbA is conserved, we observe the trans/cis isomerization of P31 in the active site and further conformational changes in the so-called "peptide binding groove" region. Interestingly, these modifications involve residues that are specific to DsbA but not to the thioredoxin family fold. The C33A crystal structure exhibits as well a hydrophobic ligand bound close to the active site of the enzyme. The structural analysis of C33A may actually explain the peculiar behavior of this mutant in regards with its interaction with DsbB and thus provides new insights for understanding the catalytic cycle of DsbA.

PubMed: 15755450
DOI: 10.1016/j.jmb.2005.01.049

実験手法

X-RAY DIFFRACTION (2.6 Å)