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M705511200v1
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Papers In Press, published online ahead of print September 19, 2007
J. Biol. Chem, 10.1074/jbc.M705511200
Submitted on July 5, 2007
Revised on September 10, 2007
Accepted on September 19, 2007

A family 2 pectate lyase displays a rare fold and transition metal-assisted beta-elimination

D. Wade Abbott and Alisdair B. Boraston

Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6

Corresponding Author: boraston{at}uvic.ca

The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved to 1.5 Å, reveals it to be the first prokaryotic protein reported to display the rare (alpha /alpha )7 barrel fold. In addition to its apo-form, we have also determined the structure of a metal-bound form of YePL2A (to 2.0 Å) and a trigalacturonic acid bound substrate complex (to 2.1 Å). Although its fold is very rare, the catalytic centre of YePL2A can be superimposed with structurally unrelated families, underlining the conserved catalytic amino acid architecture of the beta -elimination mechanism. In addition to its overall structure, YePL2A also has two other unique features: (1) it utilizes a metal atom other than calcium for catalysis and (2) its Brønstead base is in an alternate conformation and directly interacts with the uronate group of the substrate.


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