379d
From Proteopedia
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|PDB= 379d |SIZE=350|CAPTION= <scene name='initialview01'>379d</scene>, resolution 3.100Å | |PDB= 379d |SIZE=350|CAPTION= <scene name='initialview01'>379d</scene>, resolution 3.100Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT (II) ION'>CO</scene> | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</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=379d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=379d OCA], [http://www.ebi.ac.uk/pdbsum/379d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=379d RCSB]</span> | ||
}} | }} | ||
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[[Category: Terwey, D P.]] | [[Category: Terwey, D P.]] | ||
[[Category: Usman, N.]] | [[Category: Usman, N.]] | ||
| - | [[Category: CO]] | ||
[[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 05:21:59 2008'' |
Revision as of 02:22, 31 March 2008
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| , resolution 3.100Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURAL BASIS OF HAMMERHEAD RIBOZYME SELF-CLEAVAGE
Overview
We have captured an 8.7 A conformational change that takes place in the cleavage site of the hammerhead ribozyme during self-cleavage, using X-ray crystallography combined with physical and chemical trapping techniques. This rearrangement brings the hammerhead ribozyme from the ground state into a conformation that is poised to form the transition state geometry required for hammerhead RNA self-cleavage. Use of a 5'-C-methylated ribose adjacent to the cleavage site permits this ordinarily transient conformational change to be kinetically trapped and observed crystallographically after initiating the hammerhead ribozyme reaction in the crystal. Cleavage of the corresponding unmodified hammerhead ribozyme in the crystal under otherwise identical conditions is faster than in solution, indicating that we have indeed trapped a catalytically relevant intermediate form of this RNA enzyme.
About this Structure
379D is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
The structural basis of hammerhead ribozyme self-cleavage., Murray JB, Terwey DP, Maloney L, Karpeisky A, Usman N, Beigelman L, Scott WG, Cell. 1998 Mar 6;92(5):665-73. PMID:9506521
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