MF7000822 DcpS with m7GpppG 1st0 X-ray 1.90 Homodimer Homo sapiens 15068804 Gu M, Fabrega C, Liu SW, Liu H, Kiledjian M, Lima CD Mol. Cell 2004 1 14 67-80 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. GO:0140932 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity GO:0042802 identical protein binding GO:0000340 RNA 7-methylguanosine cap binding GO:0004532 RNA exonuclease activity GO:0005737 cytoplasm GO:0005829 cytosol GO:0005739 mitochondrion GO:0005654 nucleoplasm GO:0005634 nucleus GO:0000932 P-body GO:0000290 deadenylation-dependent decapping of nuclear-transcribed mRNA GO:0045292 mRNA cis splicing, via spliceosome GO:0110156 mRNA methylguanosine-cap decapping GO:0000288 nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay 2 1 Homooligomeric enzymes Homodimeric enzymes All chains according to the most probable oligomerization state stored in PDBe were considered. A m7GpppX diphosphatase Homo sapiens Q96C86 38 337 89% MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS 337 secondary structure helix 90 99 secondary structure helix 121 125 secondary structure helix 136 144 secondary structure helix 154 161 secondary structure helix 165 170 secondary structure helix 173 181 secondary structure helix 185 189 secondary structure helix 229 233 secondary structure helix 234 236 secondary structure helix 237 257 secondary structure helix 259 261 secondary structure helix 298 308 secondary structure helix 310 315 secondary structure helix 325 334 secondary structure strand 48 56 secondary structure strand 61 68 secondary structure strand 78 86 secondary structure strand 103 110 secondary structure strand 113 119 secondary structure strand 127 132 secondary structure strand 148 153 secondary structure strand 191 193 secondary structure strand 200 204 secondary structure strand 217 222 secondary structure strand 263 268 secondary structure strand 277 282 secondary structure strand 295 297 secondary structure strand 317 322 pfam PF11969 Scavenger mRNA decapping enzyme C-term binding 174 292 B m7GpppX diphosphatase Homo sapiens Q96C86 40 336 88% MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS 337 secondary structure helix 90 100 secondary structure helix 121 125 secondary structure helix 136 144 secondary structure helix 154 161 secondary structure helix 161 168 secondary structure helix 173 181 secondary structure helix 185 189 secondary structure helix 229 233 secondary structure helix 234 236 secondary structure helix 237 257 secondary structure helix 259 261 secondary structure helix 298 308 secondary structure helix 310 315 secondary structure helix 325 336 secondary structure strand 48 56 secondary structure strand 61 68 secondary structure strand 78 86 secondary structure strand 104 110 secondary structure strand 113 118 secondary structure strand 127 132 secondary structure strand 148 153 secondary structure strand 191 193 secondary structure strand 200 204 secondary structure strand 217 222 secondary structure strand 263 268 secondary structure strand 277 282 secondary structure strand 295 297 secondary structure strand 317 322 pfam PF11969 Scavenger mRNA decapping enzyme C-term binding 174 292 Indirect evidence Only some parts of the structure participates in mutual synergistic folding. Scavenger mRNA decapping enzyme (DcpS) Multidomain structure, where the domain-swapped N-terminal domain is responsible for dimerization. The extensive interface, symmetry, topology, beta sheet augmentation and buried surface area suggest that the N-terminal dimerization domain behaves as a single rigid domain and the monomers would not be stable on their own. Gel-filtration chromatography also suggested a dimeric form (PMID:15068804). B N/A A N/A MF7000822 MF7000823 MF7000824 MF7000825 MF7000826 MF7000827 MF7000828 MF7000829