Structure of pectate lyase A: comparison to other isoforms
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1.
University of Missouri–Kansas City
Abstract
Pectate lyase A is a virulence factor secreted by the plant-pathogenic bacteria Erwinia chrysanthemi. The enzyme cleaves the glycosidic bond of pectate polymers by a calcium-dependent [beta]-elimination mechanism. The crystal structure of pectate lyase A from E. chrysanthemi EC16 has been determined in two crystal forms, monoclinic C2 to 1.8 Å and rhombohedral R3 to 2.1 Å. The protein structure is compared with two other pectate lyase isoforms from E. chrysanthemi EC16, pectate lyase C and pectate lyase E. Pectate lyase A is unique as it is the only acidic pectate lyase and has end products that are significantly more varied in length in comparison to those of the other four major pectate lyase isozymes. Differences and similarities in polypeptide trace, size and volume of the active-site groove and surface electrostatics are discussed.
Additional Information
© 2002 International Union of Crystallography. Received 5 December 2001; Accepted 2 April 2002. The high-expression construct of PelA was graciously provided by Noel T. Keen. We are indebted to Chris Snook and Lesa Beamer for collecting X-ray data of the C2 crystal form at the National Synchrotron Light Source at Brookhaven National Laboratory, beamline X8C. Coordinates of PelE and the PelC±pentagalacturonate structures were graciously provided by Frances Jurnak. This work is supported by a grant from the National Science Foundation (MDY).Attached Files
Published - gr2232.pdf
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Additional details
Identifiers
- Eprint ID
- 76506
- Resolver ID
- CaltechAUTHORS:20170411-102104351
Funding
- NSF
Dates
- Created
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2017-04-11Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field