6vcp: Difference between revisions

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<StructureSection load='6vcp' size='340' side='right'caption='[[6vcp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='6vcp' size='340' side='right'caption='[[6vcp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6vcp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco45 Eco45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VCP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VCP FirstGlance]. <br>
<table><tr><td colspan='2'>[[6vcp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_S88 Escherichia coli S88]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VCP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6vcn|6vcn]], [[6vco|6vco]], [[6vck|6vck]], [[6vcl|6vcl]], [[6vcm|6vcm]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UTP:URIDINE+5-TRIPHOSPHATE'>UTP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rppH, nudH, ygdP, b2830, JW2798 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585035 ECO45])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vcp OCA], [https://pdbe.org/6vcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vcp RCSB], [https://www.ebi.ac.uk/pdbsum/6vcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vcp ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vcp OCA], [http://pdbe.org/6vcp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vcp RCSB], [http://www.ebi.ac.uk/pdbsum/6vcp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vcp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[https://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>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Eco45]]
[[Category: Escherichia coli S88]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Duan, W]]
[[Category: Duan W]]
[[Category: Gao, A]]
[[Category: Gao A]]
[[Category: Kaushik, A]]
[[Category: Kaushik A]]
[[Category: Serganov, A]]
[[Category: Serganov A]]
[[Category: Vasilyev, N]]
[[Category: Vasilyev N]]
[[Category: Rna binding protein]]
[[Category: Rna degradation]]
Retrieved from "https://proteopedia.org/6vcp"