Role of Coupled Domain Motions on the Catalytic Activity of Escherichia coli Prolyl-tRNA Synthetase.

dc.contributor.advisor	Hati, Sanchita
dc.contributor.author	Cao, Bach
dc.contributor.author	Greene, Alexander J.
dc.contributor.author	Zimmerman, Kurt A.
dc.date.accessioned	2009-09-04T14:17:35Z
dc.date.available	2009-09-04T14:17:35Z
dc.date.issued	2009-04
dc.description	Color poster with text, images, chart and diagrams.	en
dc.description.abstract	Prolyl-tRNA synthetases (ProRSs), which are class II synthetases that catalyze covalent attachment of proline to the 3'end of the tRNAPro. ProRSs from all three kingdoms of life, have shown to misactivate noncognate alanine and cysteine, and form mischarged aminoacyl?tRNAPro. It has been found that the insertion domain (?180 amino acids) of Escherichia coli (Ec) ProRS is the post-transfer editing active site that hydrolyzes specifically mischarged alanyl-tRNAPro. Herein, we report the effect of mutations on highly conserved residues (G217 and E218) located on the loop connecting the catalytic and editing domains of Ec ProRS.	en
dc.description.sponsorship	University of Wisconsin--Eau Claire Office of Research and Sponsored Programs. Research Corporation CCSA Grant. National Institutes of Health (U.S.) AREA Grant.	en
dc.identifier.uri	http://digital.library.wisc.edu/1793/36123
dc.language.iso	en_US	en
dc.relation.ispartofseries	USGZE AS589	en
dc.subject	Posters	en
dc.subject	Catalytic RNA	en
dc.subject	Escherichia coli	en
dc.subject	Ligases	en
dc.title	Role of Coupled Domain Motions on the Catalytic Activity of Escherichia coli Prolyl-tRNA Synthetase.	en
dc.type	Presentation	en

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