1ST4: Structure Of Dcps Bound To M7gpppa

Citation:
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.
PDB ID: 1ST4Download
MMDB ID: 27446
PDB Deposition Date: 2004/3/24
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.02  Å
Source Organism:
Similar Structures:
Biological Unit for 1ST4: dimeric; determined by author and by software (PISA)
Molecular Components in 1ST4
Label Count Molecule
Proteins (2 molecules)
2
mRNA Decapping Enzyme(Gene symbol: DCPS)
Molecule annotation
Chemicals (5 molecules)
1
2
2
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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