1zfv

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|PDB= 1zfv |SIZE=350|CAPTION= <scene name='initialview01'>1zfv</scene>, resolution 2.40&Aring;
|PDB= 1zfv |SIZE=350|CAPTION= <scene name='initialview01'>1zfv</scene>, resolution 2.40&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=NCO:COBALT HEXAMMINE ION'>NCO</scene>
+
|LIGAND= <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=NCO:COBALT+HEXAMMINE+ION'>NCO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1x9c|1X9C]], [[1x9k|1X9K]], [[1zfr|1ZFR]], [[1zft|1ZFT]], [[1zfx|1ZFX]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zfv OCA], [http://www.ebi.ac.uk/pdbsum/1zfv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zfv RCSB]</span>
}}
}}
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Wedekind, J E.]]
[[Category: Wedekind, J E.]]
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[[Category: NCO]]
 
-
[[Category: SO4]]
 
[[Category: all-rna]]
[[Category: all-rna]]
[[Category: catalytic rna]]
[[Category: catalytic rna]]
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[[Category: s-turn]]
[[Category: s-turn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:35:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:35:28 2008''

Revision as of 22:35, 30 March 2008


PDB ID 1zfv

Drag the structure with the mouse to rotate
, resolution 2.40Å
Ligands: , , , , ,
Related: 1X9C, 1X9K, 1ZFR, 1ZFT, 1ZFX


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The structure of an all-RNA minimal Hairpin Ribozyme with Mutation G8A at the cleavage site


Overview

The hairpin ribozyme requires functional group contributions from G8 to assist in phosphodiester bond cleavage. Previously, replacement of G8 by a series of nucleobase variants showed little effect on interdomain docking, but a 3-250-fold effect on catalysis. To identify G8 features that contribute to catalysis within the hairpin ribozyme active site, structures for five base variants were determined by X-ray crystallography in a resolution range between 2.3 and 2.7 A. For comparison, a native all-RNA "G8" hairpin ribozyme structure was refined to 2.05 A resolution. The native structure revealed a scissile bond angle (tau) of 158 degrees, which is close to the requisite 180 degrees "in-line" geometry. Mutations G8(inosine), G8(diaminopurine), G8(aminopurine), G8(adenosine), and G8(uridine) folded properly, but exhibited nonideal scissile bond geometries (tau ranging from 118 degrees to 93 degrees) that paralleled their diminished solution activities. A superposition ensemble of all structures, including a previously described hairpin ribozyme-vanadate complex, indicated the scissile bond can adopt a variety of conformations resulting from perturbation of the chemical environment and provided a rationale for how the exocyclic amine of nucleobase 8 promotes productive, in-line geometry. Changes at position 8 also caused variations in the A-1 sugar pucker. In this regard, variants A8 and U8 appeared to represent nonproductive ground states in which their 2'-OH groups mimicked the pro-R, nonbridging oxygen of the vanadate transition-state complex. Finally, the results indicated that ordered water molecules bind near the 2'-hydroxyl of A-1, lending support to the hypothesis that solvent may play an important role in the reaction.

About this Structure

1ZFV is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Water in the active site of an all-RNA hairpin ribozyme and effects of Gua8 base variants on the geometry of phosphoryl transfer., Salter J, Krucinska J, Alam S, Grum-Tokars V, Wedekind JE, Biochemistry. 2006 Jan 24;45(3):686-700. PMID:16411744

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