2c0b: Difference between revisions
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|PDB= 2c0b |SIZE=350|CAPTION= <scene name='initialview01'>2c0b</scene>, resolution 3.18Å | |PDB= 2c0b |SIZE=350|CAPTION= <scene name='initialview01'>2c0b</scene>, resolution 3.18Å | ||
|SITE= <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+L'>AC2</scene> | |SITE= <scene name='pdbsite=AC2:Zn+Binding+Site+For+Chain+L'>AC2</scene> | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0b OCA], [http://www.ebi.ac.uk/pdbsum/2c0b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c0b RCSB]</span> | |||
}} | }} | ||
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[[Category: Marcaida, M J.]] | [[Category: Marcaida, M J.]] | ||
[[Category: Scott, W G.]] | [[Category: Scott, W G.]] | ||
[[Category: endonuclease]] | [[Category: endonuclease]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: rna-binding]] | [[Category: rna-binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:14:26 2008'' | ||
Revision as of 02:14, 31 March 2008
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| , resolution 3.18Å | |||||||
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| Ligands: | , , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTIC DOMAIN OF E. COLI RNASE E IN COMPLEX WITH 13-MER RNA
OverviewOverview
The coordinated regulation of gene expression is required for homeostasis, growth and development in all organisms. Such coordination may be partly achieved at the level of messenger RNA stability, in which the targeted destruction of subsets of transcripts generates the potential for cross-regulating metabolic pathways. In Escherichia coli, the balance and composition of the transcript population is affected by RNase E, an essential endoribonuclease that not only turns over RNA but also processes certain key RNA precursors. RNase E cleaves RNA internally, but its catalytic power is determined by the 5' terminus of the substrate, even if this lies at a distance from the cutting site. Here we report crystal structures of the catalytic domain of RNase E as trapped allosteric intermediates with RNA substrates. Four subunits of RNase E catalytic domain associate into an interwoven quaternary structure, explaining why the subunit organization is required for catalytic activity. The subdomain encompassing the active site is structurally congruent to a deoxyribonuclease, making an unexpected link in the evolutionary history of RNA and DNA nucleases. The structure explains how the recognition of the 5' terminus of the substrate may trigger catalysis and also sheds light on the question of how RNase E might selectively process, rather than destroy, specific RNA precursors.
About this StructureAbout this Structure
2C0B is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover., Callaghan AJ, Marcaida MJ, Stead JA, McDowall KJ, Scott WG, Luisi BF, Nature. 2005 Oct 20;437(7062):1187-91. PMID:16237448
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