1CKN

STRUCTURE OF GUANYLYLATED MRNA CAPPING ENZYME COMPLEXED WITH GTP

Summary for 1CKN

• Entry DOI: 10.2210/pdb1ckn/pdb
• Descriptor: MRNA CAPPING ENZYME, GUANOSINE-5'-TRIPHOSPHATE, MANGANESE (II) ION, ... (6 entities in total)
• Functional Keywords: mrna, capping enzyme, nucleotidyltransferase
• Biological source: Paramecium bursaria Chlorella virus 1; More
• Total number of polymer chains: 2
• Total formula weight: 76788.36

Authors

Hakansson, K.,Doherty, A.J.,Wigley, D.B. (deposition date: 1997-04-20, release date: 1997-07-07, Last modification date: 2023-08-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)