skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Crystal Structure of Mn2+-bound Escherichia coli L-arabinose Isomerase (ECAI) and Implications in Protein Catalytic Mechanism and Thermo-Stability

Abstract

The functional properties of proteins depend on their three-dimensional shapes. Protein structures can be determined by X-ray crystallography as a tool. The three-dimensional structure of the apo form of the Escherichia coli L-arabinose isomerase (ECAI) has recently been determined. ECAI is responsible for the initial stage of L-arabinose catabolism, converting arabinose into ribulose in vivo. This enzyme also plays a crucial role in catalyzing the conversion of galactose into tagatose (low calorie natural sugar) in vitro. ECAI utilizes Mn{sup 2+} for its catalytic activity. Crystals of the ECAI + Mn{sup 2+} complex helps to investigate the catalytic properties of the enzyme. Therefore, crystals of ECAI + Mn{sup 2+} complex were grown using hanging drop vapor diffusion method at room temperature. Diffraction data were collected at X4C beamline, National Synchrotron Light Source, Brookhaven National Laboratory. The structure was solved by the molecular replacement technique and has been refined to Rwork of 0.23 at 2.8 {angstrom} resolution using X3A beamline computational facility. The structure was deposited to Protein Data Bank (PDB ID 2HXG). Mn{sup 2+} ion was localized to the previously identified putative active site with octahedral coordination. Comparison of apo and holo form of ECAI structures permits the identification of structuralmore » features that are of importance to the intrinsic activity and heat stability of AI.« less

Authors:
; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930523
Report Number(s):
BNL-80530-2008-JA
Journal ID: ISSN 1470-8175; TRN: US0901406
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Young Investigators; Journal Volume: 17; Journal Issue: 3
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; 43 PARTICLE ACCELERATORS; ARABINOSE; BNL; CATABOLISM; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DIFFRACTION; DIFFUSION; ENZYMES; ESCHERICHIA COLI; FUNCTIONALS; GALACTOSE; IN VITRO; IN VIVO; ISOMERASES; NSLS; PROTEIN STRUCTURE; PROTEINS; RESOLUTION; RIBULOSE; SACCHAROSE; SENSITIVITY; THERMAL DEGRADATION; national synchrotron light source

Citation Formats

Zhu,W., Manjasetty, B., and Chance, M. Crystal Structure of Mn2+-bound Escherichia coli L-arabinose Isomerase (ECAI) and Implications in Protein Catalytic Mechanism and Thermo-Stability. United States: N. p., 2007. Web.
Zhu,W., Manjasetty, B., & Chance, M. Crystal Structure of Mn2+-bound Escherichia coli L-arabinose Isomerase (ECAI) and Implications in Protein Catalytic Mechanism and Thermo-Stability. United States.
Zhu,W., Manjasetty, B., and Chance, M. Mon . "Crystal Structure of Mn2+-bound Escherichia coli L-arabinose Isomerase (ECAI) and Implications in Protein Catalytic Mechanism and Thermo-Stability". United States. doi:.
@article{osti_930523,
title = {Crystal Structure of Mn2+-bound Escherichia coli L-arabinose Isomerase (ECAI) and Implications in Protein Catalytic Mechanism and Thermo-Stability},
author = {Zhu,W. and Manjasetty, B. and Chance, M.},
abstractNote = {The functional properties of proteins depend on their three-dimensional shapes. Protein structures can be determined by X-ray crystallography as a tool. The three-dimensional structure of the apo form of the Escherichia coli L-arabinose isomerase (ECAI) has recently been determined. ECAI is responsible for the initial stage of L-arabinose catabolism, converting arabinose into ribulose in vivo. This enzyme also plays a crucial role in catalyzing the conversion of galactose into tagatose (low calorie natural sugar) in vitro. ECAI utilizes Mn{sup 2+} for its catalytic activity. Crystals of the ECAI + Mn{sup 2+} complex helps to investigate the catalytic properties of the enzyme. Therefore, crystals of ECAI + Mn{sup 2+} complex were grown using hanging drop vapor diffusion method at room temperature. Diffraction data were collected at X4C beamline, National Synchrotron Light Source, Brookhaven National Laboratory. The structure was solved by the molecular replacement technique and has been refined to Rwork of 0.23 at 2.8 {angstrom} resolution using X3A beamline computational facility. The structure was deposited to Protein Data Bank (PDB ID 2HXG). Mn{sup 2+} ion was localized to the previously identified putative active site with octahedral coordination. Comparison of apo and holo form of ECAI structures permits the identification of structural features that are of importance to the intrinsic activity and heat stability of AI.},
doi = {},
journal = {Journal of Young Investigators},
number = 3,
volume = 17,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}