1LBA

THE STRUCTURE OF BACTERIOPHAGE T7 LYSOZYME, A ZINC AMIDASE AND AN INHIBITOR OF T7 RNA POLYMERASE

1LBA の概要

• エントリーDOI: 10.2210/pdb1lba/pdb
• 分子名称: T7 LYSOZYME, ZINC ION (3 entities in total)
• 機能のキーワード: hydrolase(acting on linear amides)
• 由来する生物種: Enterobacteria phage T7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16409.89

構造登録者

Cheng, X. (登録日: 1993-12-22, 公開日: 1994-04-30, 最終更新日: 2024-02-14)

主引用文献

Cheng, X.,Zhang, X.,Pflugrath, J.W.,Studier, F.W.
The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase.
Proc.Natl.Acad.Sci.USA, 91:4034-4038, 1994

PubMed Abstract: The lysozyme of bacteriophage T7 is a bifunctional protein that cuts amide bonds in the bacterial cell wall and binds to and inhibits transcription by T7 RNA polymerase. The structure of a mutant T7 lysozyme has been determined by x-ray crystallography and refined at 2.2-A resolution. The protein folds into an alpha/beta-sheet structure that has a prominent cleft. A zinc atom is located in the cleft, bound directly to three amino acids and, through a water molecule, to a fourth. Zinc is required for amidase activity but not for inhibition of T7 RNA polymerase. Alignment of the zinc ligands of T7 lysozyme with those of carboxypeptidase A and thermolysin suggests structural similarity among the catalytic sites for the amidase and these zinc proteases. Mutational analysis identified presumed catalytic residues for amidase activity within the cleft and a surface that appears to be the site of binding to T7 RNA polymerase. Binding of T7 RNA polymerase inhibits amidase activity.

PubMed: 8171031
DOI: 10.1073/pnas.91.9.4034

実験手法

X-RAY DIFFRACTION (2.2 Å)