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2vrt

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Revision as of 08:26, 25 June 2020

Crystal Structure of E. coli RNase E possessing M1 RNA fragments - Catalytic Domain

Structural highlights

2vrt is a 8 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2bx2, 2c0b, 2vmk, 2c4r, 1slj, 1sn8, 2fym, 1smx
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RNE_ECOLI] Matures 5S rRNA from its precursors from all the rRNA genes. It also cleaves RNA I, a molecule that controls the replication of colE1 plasmid DNA. It is the major endoribonuclease participating in mRNA turnover in E.coli. It initiates the decay of RNAs by cutting them internally near their 5'-end. It is able to remove poly(A) tails by an endonucleolytic process.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli. Here, we present the crystal structure of the E. coli RNase E catalytic domain in the apo-state at 3.3 A. This structure indicates that, upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site. The structural data suggest a mechanism of RNA recognition and cleavage that explains the enzyme's preference for substrates possessing a 5'-monophosphate and accounts for the protective effect of a triphosphate cap for most transcripts. Internal flexibility within the quaternary structure is also observed, a finding that has implications for recognition of structured RNA substrates and for the mechanism of internal entry for a subset of substrates that are cleaved without 5'-end requirements.

The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation.,Koslover DJ, Callaghan AJ, Marcaida MJ, Garman EF, Martick M, Scott WG, Luisi BF Structure. 2008 Aug 6;16(8):1238-44. PMID:18682225^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Koslover DJ, Callaghan AJ, Marcaida MJ, Garman EF, Martick M, Scott WG, Luisi BF. The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation. Structure. 2008 Aug 6;16(8):1238-44. PMID:18682225 doi:10.1016/j.str.2008.04.017

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vrt"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of E. coli RNase E possessing M1 RNA fragments - Catalytic Domain==
-<StructureSection load='2vrt' size='340' side='right' caption='[[2vrt]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+<StructureSection load='2vrt' size='340' side='right'caption='[[2vrt]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vrt]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VRT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vrt]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VRT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bx2|2bx2]], [[2c0b|2c0b]], [[2vmk|2vmk]], [[2c4r|2c4r]], [[1slj|1slj]], [[1sn8|1sn8]], [[2fym|2fym]], [[1smx|1smx]]</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=2vrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrt OCA], [http://pdbe.org/2vrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vrt RCSB], [http://www.ebi.ac.uk/pdbsum/2vrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrt 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=2vrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrt OCA], [http://pdbe.org/2vrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vrt RCSB], [http://www.ebi.ac.uk/pdbsum/2vrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrt ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Ribonuclease|Ribonuclease]]
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 *[[Temp|Temp]]
 *[[Temperature value vs. resolution|Temperature value vs. resolution]]
@@ Line 39: / Line 39: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Callaghan, A J]]
 [[Category: Garman, E F]]

2vrt

From Proteopedia

Revision as of 08:26, 25 June 2020

Crystal Structure of E. coli RNase E possessing M1 RNA fragments - Catalytic Domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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