488d

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[[Image:488d.gif|left|200px]]
[[Image:488d.gif|left|200px]]
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{{Structure
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|PDB= 488d |SIZE=350|CAPTION= <scene name='initialview01'>488d</scene>, resolution 3.10&Aring;
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The line below this paragraph, containing "STRUCTURE_488d", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=CCC:CYTIDINE-5&#39;-PHOSPHATE-2&#39;,3&#39;-CYCLIC+PHOSPHATE'>CCC</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
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|ACTIVITY=
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|GENE=
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|DOMAIN=
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{{STRUCTURE_488d| PDB=488d | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=488d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=488d OCA], [http://www.ebi.ac.uk/pdbsum/488d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=488d RCSB]</span>
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}}
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'''CATALYTIC RNA ENZYME-PRODUCT COMPLEX'''
'''CATALYTIC RNA ENZYME-PRODUCT COMPLEX'''
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==About this Structure==
==About this Structure==
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488D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=488D OCA].
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=488D OCA].
==Reference==
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/10882069 10882069]
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://www.ncbi.nlm.nih.gov/pubmed/10882069 10882069]
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[[Category: Protein complex]]
 
[[Category: Murray, J B.]]
[[Category: Murray, J B.]]
[[Category: Scott, W G.]]
[[Category: Scott, W G.]]
[[Category: Szoke, A.]]
[[Category: Szoke, A.]]
[[Category: Szoke, H.]]
[[Category: Szoke, H.]]
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[[Category: catalytic rna]]
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[[Category: Catalytic rna]]
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[[Category: crystal lattice trapping]]
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[[Category: Crystal lattice trapping]]
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[[Category: enzyme-product complex]]
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[[Category: Enzyme-product complex]]
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[[Category: ribozyme]]
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[[Category: Ribozyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:20:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:37:51 2008''
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Revision as of 19:20, 4 May 2008

Image:488d.gif

Template:STRUCTURE 488d

CATALYTIC RNA ENZYME-PRODUCT COMPLEX


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.

About this Structure

Full crystallographic information is available from OCA.

Reference

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:10882069 Page seeded by OCA on Sun May 4 22:20:13 2008

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