301d
From Proteopedia
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|PDB= 301d |SIZE=350|CAPTION= <scene name='initialview01'>301d</scene>, resolution 3.000Å | |PDB= 301d |SIZE=350|CAPTION= <scene name='initialview01'>301d</scene>, resolution 3.000Å | ||
|SITE= | |SITE= | ||
| - | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=301d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=301d OCA], [http://www.ebi.ac.uk/pdbsum/301d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=301d RCSB]</span> | ||
}} | }} | ||
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[[Category: Scott, W G.]] | [[Category: Scott, W G.]] | ||
[[Category: Stoddard, B L.]] | [[Category: Stoddard, B L.]] | ||
| - | [[Category: MG]] | ||
[[Category: catalytic rna]] | [[Category: catalytic rna]] | ||
[[Category: loop]] | [[Category: loop]] | ||
[[Category: rna hammerhead ribozyme]] | [[Category: rna hammerhead ribozyme]] | ||
| - | ''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 05:21:03 2008'' |
Revision as of 02:21, 31 March 2008
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| , resolution 3.000Å | |||||||
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| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CAPTURING THE STRUCTURE OF A CATALYTIC RNA INTERMEDIATE: RNA HAMMERHEAD RIBOZYME, MG(II)-SOAKED
Overview
The crystal structure of an unmodified hammerhead RNA in the absence of divalent metal ions has been solved, and it was shown that this ribozyme can cleave itself in the crystal when divalent metal ions are added. This biologically active RNA fold is the same as that found previously for two modified hammerhead ribozymes. Addition of divalent cations at low pH makes it possible to capture the uncleaved RNA in metal-bound form. A conformational intermediate, having an additional Mg(II) bound to the cleavage-site phosphate, was captured by freeze-trapping the RNA at an active pH prior to cleavage. The most significant conformational changes were limited to the active site of the ribozyme, and the changed conformation requires only small additional movements to reach a proposed transition-state.
About this Structure
301D is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Capturing the structure of a catalytic RNA intermediate: the hammerhead ribozyme., Scott WG, Murray JB, Arnold JR, Stoddard BL, Klug A, Science. 1996 Dec 20;274(5295):2065-9. PMID:8953035
Page seeded by OCA on Mon Mar 31 05:21:03 2008
