1CKN

STRUCTURE OF GUANYLYLATED MRNA CAPPING ENZYME COMPLEXED WITH GTP

1CKN の概要

• エントリーDOI: 10.2210/pdb1ckn/pdb
• 分子名称: MRNA CAPPING ENZYME, GUANOSINE-5'-TRIPHOSPHATE, MANGANESE (II) ION, ... (6 entities in total)
• 機能のキーワード: mrna, capping enzyme, nucleotidyltransferase
• 由来する生物種: Paramecium bursaria Chlorella virus 1; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76788.36

構造登録者

Hakansson, K.,Doherty, A.J.,Wigley, D.B. (登録日: 1997-04-20, 公開日: 1997-07-07, 最終更新日: 2023-08-09)

主引用文献

Hakansson, K.,Doherty, A.J.,Shuman, S.,Wigley, D.B.
X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes.
Cell(Cambridge,Mass.), 89:545-553, 1997

PubMed Abstract: We have solved the crystal structure of an mRNA capping enzyme at 2.5 A resolution. The enzyme comprises two domains with a deep, but narrow, cleft between them. The two molecules in the crystallographic asymmetric unit adopt very different conformations; both contain a bound GTP, but one protein molecule is in an open conformation while the other is in a closed conformation. Only in the closed conformation is the enzyme able to bind manganese ions and undergo catalysis within the crystals to yield the covalent guanylated enzyme intermediate. These structures provide direct evidence for a mechanism that involves a significant conformational change in the enzyme during catalysis.

PubMed: 9160746
DOI: 10.1016/S0092-8674(00)80236-6

実験手法

X-RAY DIFFRACTION (2.5 Å)