Motion in mRNA capping enzyme [mrnacap]

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Classification [D-h-2]

Structures
1CKM Both forms [ PartsList ]

Description
From Hakansson et al. (1997): "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."

References
K Håkansson, A J Doherty, S Shuman, D B Wigley (1997). X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell, 89:545-53 [Medline info for 9160746]
Hakansson, K., Wigley, D. B.: Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping. Proc Natl Acad Sci U S A 95 pp. 1505 (1998) [Medline info for 9465045]

GO terms associated with structures
Molecular functionmRNA guanylyltransferase activity
Biological processmRNA capping, mRNA processing

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
capping enzyme 1CKM [ A ] 1CKM [ B ] 317



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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu