429d
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(New page: 200px<br /><applet load="429d" size="350" color="white" frame="true" align="right" spinBox="true" caption="429d, resolution 2.70Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 19:43, 29 January 2008
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CRYSTAL STRUCTURE OF A LEADZYME; METAL BINDING AND IMPLICATIONS FOR CATALYSIS
Overview
The leadzyme is a small RNA motif that catalyzes a site-specific, Pb2+-dependent cleavage reaction. As such, it is an example of a, metal-dependent RNA enzyme. Here we describe the X-ray crystallographic, structure of the leadzyme, which reveals two independent molecules per, asymmetric unit. Both molecules feature an internal loop in which a bulged, purine base stack twists away from the helical stem. This kinks the, backbone, rendering the phosphodiester bond susceptible to cleavage. The, independent molecules have different conformations: one leadzyme copy, coordinates Mg2+, whereas the other binds only Ba2+ or Pb2+. In the active, site of the latter molecule, a single Ba2+ ion coordinates the 2'-OH, nucleophile, and appears to mimic the binding of catalytic lead. These, observations allow a bond cleavage reaction to be modeled, which reveals, the minimal structural features necessary for catalysis by this small, ribozyme.
About this Structure
429D is a Protein complex structure of sequences from [1] with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a lead-dependent ribozyme revealing metal binding sites relevant to catalysis., Wedekind JE, McKay DB, Nat Struct Biol. 1999 Mar;6(3):261-8. PMID:10074945
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