2ffl: Difference between revisions

Revision as of 18:20, 21 February 2008

Crystal Structure of Dicer from Giardia intestinalis

OverviewOverview

The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.

About this StructureAbout this Structure

2FFL is a Single protein structure of sequence from Giardia intestinalis with as ligand. Active as Ribonuclease III, with EC number 3.1.26.3 Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for double-stranded RNA processing by Dicer., Macrae IJ, Zhou K, Li F, Repic A, Brooks AN, Cande WZ, Adams PD, Doudna JA, Science. 2006 Jan 13;311(5758):195-8. PMID:16410517

Page seeded by OCA on Thu Feb 21 17:20:55 2008

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OCA

@@ Line 4: / Line 4: @@
 ==Overview==
-The specialized ribonuclease Dicer initiates RNA interference by cleaving, double-stranded RNA (dsRNA) substrates into small fragments about 25, nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from, the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and, RNase III domains matches the length spanned by 25 base pairs of RNA., Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves, a specified distance from the helical end.
+The specialized ribonuclease Dicer initiates RNA interference by cleaving double-stranded RNA (dsRNA) substrates into small fragments about 25 nucleotides in length. In the crystal structure of an intact Dicer enzyme, the PAZ domain, a module that binds the end of dsRNA, is separated from the two catalytic ribonuclease III (RNase III) domains by a flat, positively charged surface. The 65 angstrom distance between the PAZ and RNase III domains matches the length spanned by 25 base pairs of RNA. Thus, Dicer itself is a molecular ruler that recognizes dsRNA and cleaves a specified distance from the helical end.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Ribonuclease III]]
 [[Category: Single protein]]
-[[Category: Adams, P.D.]]
+[[Category: Adams, P D.]]
-[[Category: Doudna, J.A.]]
+[[Category: Doudna, J A.]]
-[[Category: MacRae, I.J.]]
+[[Category: MacRae, I J.]]
 [[Category: MN]]
 [[Category: rna interference; rnai; paz domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:35:23 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:55 2008''