488d: Difference between revisions

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==Overview==

We have determined the crystal structure of the enzyme-product complex of, the hammerhead ribozyme by using a reinforced crystal lattice to trap the, complex prior to dissociation and by employing X-ray holographic image, reconstruction, a real-space electron density imaging and refinement, procedure. Subsequent to catalysis, the cleavage site residue (C-17), together with its 2',3'-cyclic phosphate, adopts a conformation close to, and approximately perpendicular to the Watson-Crick base-pairing faces of, two highly conserved purines in the ribozyme's catalytic pocket (G-5 and, A-6). We observe several interactions with functional groups on these, residues that have been identified as critical for ribozyme activity by, biochemical analyses but whose role has defied explanation in terms of, previous structural analyses. These interactions may therefore be relevant, to the hammerhead ribozyme reaction mechanism.

We have determined the crystal structure of the enzyme-product complex of the hammerhead ribozyme by using a reinforced crystal lattice to trap the complex prior to dissociation and by employing X-ray holographic image reconstruction, a real-space electron density imaging and refinement procedure. Subsequent to catalysis, the cleavage site residue (C-17), together with its 2',3'-cyclic phosphate, adopts a conformation close to and approximately perpendicular to the Watson-Crick base-pairing faces of two highly conserved purines in the ribozyme's catalytic pocket (G-5 and A-6). We observe several interactions with functional groups on these residues that have been identified as critical for ribozyme activity by biochemical analyses but whose role has defied explanation in terms of previous structural analyses. These interactions may therefore be relevant to the hammerhead ribozyme reaction mechanism.

==About this Structure==

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Capture and visualization of a catalytic RNA enzyme-product complex using crystal lattice trapping and X-ray holographic reconstruction., Murray JB, Szoke H, Szoke A, Scott WG, Mol Cell. 2000 Feb;5(2):279-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10882069 10882069]

[[Category: Protein complex]]

[[Category: Murray, J.B.]]

[[Category: Murray, J B.]]

[[Category: Scott, W.G.]]

[[Category: Scott, W G.]]

[[Category: Szoke, A.]]

[[Category: Szoke, H.]]

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[[Category: ribozyme]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-We have determined the crystal structure of the enzyme-product complex of, the hammerhead ribozyme by using a reinforced crystal lattice to trap the, complex prior to dissociation and by employing X-ray holographic image, reconstruction, a real-space electron density imaging and refinement, procedure. Subsequent to catalysis, the cleavage site residue (C-17), together with its 2',3'-cyclic phosphate, adopts a conformation close to, and approximately perpendicular to the Watson-Crick base-pairing faces of, two highly conserved purines in the ribozyme's catalytic pocket (G-5 and, A-6). We observe several interactions with functional groups on these, residues that have been identified as critical for ribozyme activity by, biochemical analyses but whose role has defied explanation in terms of, previous structural analyses. These interactions may therefore be relevant, to the hammerhead ribozyme reaction mechanism.
+We have determined the crystal structure of the enzyme-product complex of the hammerhead ribozyme by using a reinforced crystal lattice to trap the complex prior to dissociation and by employing X-ray holographic image reconstruction, a real-space electron density imaging and refinement procedure. Subsequent to catalysis, the cleavage site residue (C-17), together with its 2',3'-cyclic phosphate, adopts a conformation close to and approximately perpendicular to the Watson-Crick base-pairing faces of two highly conserved purines in the ribozyme's catalytic pocket (G-5 and A-6). We observe several interactions with functional groups on these residues that have been identified as critical for ribozyme activity by biochemical analyses but whose role has defied explanation in terms of previous structural analyses. These interactions may therefore be relevant to the hammerhead ribozyme reaction mechanism.
 ==About this Structure==
@@ Line 12: / Line 12: @@
 Capture and visualization of a catalytic RNA enzyme-product complex using crystal lattice trapping and X-ray holographic reconstruction., Murray JB, Szoke H, Szoke A, Scott WG, Mol Cell. 2000 Feb;5(2):279-87. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10882069 10882069]
 [[Category: Protein complex]]
-[[Category: Murray, J.B.]]
+[[Category: Murray, J B.]]
-[[Category: Scott, W.G.]]
+[[Category: Scott, W G.]]
 [[Category: Szoke, A.]]
 [[Category: Szoke, H.]]
@@ Line 22: / Line 22: @@
 [[Category: ribozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:45:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:12:40 2008''