1st0

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Revision as of 17:11, 12 November 2007

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spinqualitylabelsall models 1st0, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of DcpS bound to m7GpppG

Overview

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 Structure

1ST0 is a Single protein structure of sequence from Homo sapiens with YT3 and GTG as ligands. The following page contains interesting information on the relation of 1ST0 with [Exosomes]. Full crystallographic information is available from OCA.

Reference

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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