4s2x
From Proteopedia
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| - | ''' | + | ==Structure of E. coli RppH bound to RNA and two magnesium ions== |
| - | + | <StructureSection load='4s2x' size='340' side='right' caption='[[4s2x]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4s2x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S2X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S2X FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4s2v|4s2v]], [[4s2w|4s2w]], [[4s2y|4s2y]]</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4s2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s2x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4s2x RCSB], [http://www.ebi.ac.uk/pdbsum/4s2x PDBsum]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RPPH_ECOLI RPPH_ECOLI]] Master regulator of 5'-dependent mRNA decay. Accelerates the degradation of transcripts by removing pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a more labile monophosphorylated state that can stimulate subsequent ribonuclease cleavage. Preferentially hydrolyzes diadenosine penta-phosphate with ATP as one of the reaction products. Also able to hydrolyze diadenosine hexa- and tetra-phosphate. Has no activity on diadenosine tri-phosphate, ADP-ribose, NADH and UDP-glucose. In the meningitis causing strain E.coli K1, has been shown to play a role in HBMEC (human brain microvascular endothelial cells) invasion in vitro.<ref>PMID:10760174</ref> <ref>PMID:18202662</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Serganov, A]] | [[Category: Serganov, A]] | ||
[[Category: Vasilyev, N]] | [[Category: Vasilyev, N]] | ||
| + | [[Category: Hydrolase-rna complex]] | ||
| + | [[Category: Nudix hydrolase]] | ||
| + | [[Category: Rna pyrophosphohydrolase]] | ||
Revision as of 12:00, 12 February 2015
Structure of E. coli RppH bound to RNA and two magnesium ions
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