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Revision as of 20:36, 9 March 2012

This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439.

Contents 1 Leadzyme, 1nuv 1.1 Introduction 1.2 Overall Structure 1.3 Binding Interactions 1.4 Additional Features 1.5 Credits 1.6 References

Leadzyme, 1nuv

spinqualitylabelsall models Leadzyme 1nuv Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Introduction

Overall Structure

Leadzyme is made up of each shown in a different color. One of the RNA duplexes is shown with nucleotides 18-30 shown in orange and nucleotides 39-49 shown in blue. The duplex contains two The C23 to A45 is shown in black and A25 to G44 is shown in blue.

Binding Interactions

In the first half of a two-step reaction, the motif uses Pb2+ to cleave the phosphodiester backbone of the substrate strand, yielding a free 5ʹ′-hydroxyl and a 2ʹ′,3ʹ′-cyclic phosphodiester as products, which is analogous to the activity catalyzed by naturally occurring small ribozymes such as the hammerhead and hairpin. The cyclic phosphate is hydrolyzed subsequently to produce a 3ʹ′-phosphate in a manner similar to that of protein ribonuclease A.

Additional Features

The is dependent on the inclusion of lead for catalytic effect: no other ion gives the same result.

The addition of lanthanide ions has been found to increase the rate of substrate cleavage.

Studies show that equimolar solutions of neodymium (III) and lead (II) maximize this effect, suggesting that neodymium acts in concert with lead, as an acid catalyst. The site at which the RNA is cleaved remains unchanged.

Credits

Introduction - name of team member

Overall Structure - Adam Ramey

Drug Binding Site - name of team member

Additional Features - Tom Foley

Fill in your names please. Prof T

References