1st4
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Structure of DcpS bound to m7GpppA
OverviewOverview
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.
About this StructureAbout this Structure
1ST4 is a Single protein structure of sequence from Homo sapiens with YT3 and GTA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity., Gu M, Fabrega C, Liu SW, Liu H, Kiledjian M, Lima CD, Mol Cell. 2004 Apr 9;14(1):67-80. PMID:15068804
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