301d: Difference between revisions

Revision as of 20:01, 21 February 2008

CAPTURING THE STRUCTURE OF A CATALYTIC RNA INTERMEDIATE: RNA HAMMERHEAD RIBOZYME, MG(II)-SOAKED

OverviewOverview

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 StructureAbout this Structure

301D is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Feb 21 19:01:53 2008

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OCA

@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 12: / Line 12: @@
 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8953035 8953035]
 [[Category: Protein complex]]
-[[Category: Arnold, J.R.P.]]
+[[Category: Arnold, J R.P.]]
 [[Category: Klug, A.]]
-[[Category: Murray, J.B.]]
+[[Category: Murray, J B.]]
-[[Category: Scott, W.G.]]
+[[Category: Scott, W G.]]
-[[Category: Stoddard, B.L.]]
+[[Category: Stoddard, B L.]]
 [[Category: MG]]
 [[Category: catalytic rna]]
@@ Line 22: / Line 22: @@
 [[Category: rna hammerhead ribozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:34:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:01:53 2008''