1zbf
From Proteopedia
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[[Image:1zbf.gif|left|200px]] | [[Image:1zbf.gif|left|200px]] | ||
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'''Crystal structure of B. halodurans RNase H catalytic domain mutant D132N''' | '''Crystal structure of B. halodurans RNase H catalytic domain mutant D132N''' | ||
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[[Category: Nowotny, M.]] | [[Category: Nowotny, M.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
| - | [[Category: | + | [[Category: Dde motif]] |
| - | [[Category: | + | [[Category: Rna/dna hybrid]] |
| - | [[Category: | + | [[Category: Rnase h]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:25:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:25, 3 May 2008
Crystal structure of B. halodurans RNase H catalytic domain mutant D132N
Overview
RNase H belongs to a nucleotidyl-transferase superfamily, which includes transposase, retroviral integrase, Holliday junction resolvase, and RISC nuclease Argonaute. We report the crystal structures of RNase H complexed with an RNA/DNA hybrid and a mechanism for substrate recognition and two-metal-ion-dependent catalysis. RNase H specifically recognizes the A form RNA strand and the B form DNA strand. Structure comparisons lead us to predict the catalytic residues of Argonaute and conclude that two-metal-ion catalysis is a general feature of the superfamily. In nucleases, the two metal ions are asymmetrically coordinated and have distinct roles in activating the nucleophile and stabilizing the transition state. In transposases, they are symmetrically coordinated and exchange roles to alternately activate a water and a 3'-OH for successive strand cleavage and transfer by a ping-pong mechanism.
About this Structure
1ZBF is a Single protein structure of sequence from Bacillus halodurans. Full crystallographic information is available from OCA.
Reference
Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis., Nowotny M, Gaidamakov SA, Crouch RJ, Yang W, Cell. 2005 Jul 1;121(7):1005-16. PMID:15989951 Page seeded by OCA on Sat May 3 17:25:17 2008
