1ST4

Structure of DcpS bound to m7GpppA

Summary for 1ST4

• Entry DOI: 10.2210/pdb1st4/pdb
• Related: 1ST0
• Descriptor: mRNA decapping enzyme, P1-7-METHYLGUANOSINE-P3-ADENOSINE-5',5'-TRIPHOSPHATE, YTTRIUM (III) ION, ... (4 entities in total)
• Functional Keywords: rna decay, exosome, decapping, hit protein, messenger rna, mrna, cap, rna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q96C86
• Total number of polymer chains: 2
• Total formula weight: 79119.00

Authors

Gu, M.,Fabrega, C.,Liu, S.W.,Liu, H.,Kiledjian, M.,Lima, C.D. (deposition date: 2004-03-24, release date: 2004-04-13, Last modification date: 2023-08-23)

Primary citation

Gu, M.,Fabrega, C.,Liu, S.W.,Liu, H.,Kiledjian, M.,Lima, C.D.
Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity
Mol.Cell, 14:67-80, 2004

PubMed Abstract: Complete removal of residual N-7 guanine cap from degraded messenger RNA is necessary to prevent accumulation of intermediates that might interfere with RNA processing, export, and translation. The human scavenger decapping enzyme, DcpS, catalyzes residual cap hydrolysis following mRNA degradation, releasing N-7 methyl guanosine monophosphate and 5'-diphosphate terminated cap or mRNA products. DcpS structures bound to m(7)GpppG or m(7)GpppA reveal an asymmetric DcpS dimer that simultaneously creates an open nonproductive DcpS-cap complex and a closed productive DcpS-cap complex that alternate via 30 A domain movements. Structural and biochemical analysis suggests an autoregulatory mechanism whereby premature decapping mRNA is prevented by blocking the conformational changes that are required to form a closed productive active site capable of cap hydrolysis.

PubMed: 15068804
DOI: 10.1016/S1097-2765(04)00180-7

Experimental method

X-RAY DIFFRACTION (2.02 Å)