Event Title

Tertiary Structure and Active Sites Conformations in Forms I and II RuBisCO

Location

Parker-Reed, SSWAC

Start Date

30-4-2015 11:00 AM

End Date

30-4-2015 1:55 PM

Project Type

Poster

Description

A slow catalytic rate and poor substrate discrimination are contrasted by the essential biological role of the ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) enzyme. There are two major forms of catalytically active RuBisCO. Despite a highly conserved active site, the two forms exhibit distinct tertiary structures and sequence heterogeneity. The structure-function relationship between tertiary structure and a proposed trade-off between substrate specificity and catalytic rate is an area of focus in studies to improve RuBisCOs catalytic efficiency. We present results from molecular dynamics simulations of both forms of the activated RuBisCO enzyme. We present results of molecular dynamics simulations of activated form I and II RuBisCO enzymes and identify the inter- and intramolecular interactions that occur through thermal fluctuations.

Sponsoring Department

Colby College. Chemistry Dept.

CLAS Field of Study

Natural Sciences

Event Website

http://www.colby.edu/clas

ID

1061

Share

COinS
 
Apr 30th, 11:00 AM Apr 30th, 1:55 PM

Tertiary Structure and Active Sites Conformations in Forms I and II RuBisCO

Parker-Reed, SSWAC

A slow catalytic rate and poor substrate discrimination are contrasted by the essential biological role of the ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) enzyme. There are two major forms of catalytically active RuBisCO. Despite a highly conserved active site, the two forms exhibit distinct tertiary structures and sequence heterogeneity. The structure-function relationship between tertiary structure and a proposed trade-off between substrate specificity and catalytic rate is an area of focus in studies to improve RuBisCOs catalytic efficiency. We present results from molecular dynamics simulations of both forms of the activated RuBisCO enzyme. We present results of molecular dynamics simulations of activated form I and II RuBisCO enzymes and identify the inter- and intramolecular interactions that occur through thermal fluctuations.

http://digitalcommons.colby.edu/clas/2015/program/4