1ckn

STRUCTURE OF GUANYLYLATED MRNA CAPPING ENZYME COMPLEXED WITH GTP

spinqualitylabelsall models 1ckn, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ckn is a 2 chain structure with sequence from Paramecium bursaria Chlorella virus 1. The January 2012 RCSB PDB Molecule of the Month feature on Messenger RNA Capping by David Goodsell is 10.2210/rcsb_pdb/mom_2012_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: GPL, GTP, MN, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCE_PBCV1 mRNA capping. Transfers a GMP cap onto the end of mRNA that terminates with a 5'-diphosphate tail. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes.,Hakansson K, Doherty AJ, Shuman S, Wigley DB Cell. 1997 May 16;89(4):545-53. PMID:9160746 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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