379d: Difference between revisions

Revision as of 20:02, 21 February 2008

THE STRUCTURAL BASIS OF HAMMERHEAD RIBOZYME SELF-CLEAVAGE

OverviewOverview

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 StructureAbout this Structure

379D is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 19:02:27 2008

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OCA

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 15: / Line 15: @@
 [[Category: Karpeisky, A.]]
 [[Category: Maloney, L.]]
-[[Category: Murray, J.B.]]
+[[Category: Murray, J B.]]
-[[Category: Scott, W.G.]]
+[[Category: Scott, W G.]]
-[[Category: Terwey, D.P.]]
+[[Category: Terwey, D P.]]
 [[Category: Usman, N.]]
 [[Category: CO]]
@@ Line 24: / Line 24: @@
 [[Category: rna hammerhead ribozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:37:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:02:27 2008''