2V8J: Structure Of A Family 2 Pectate Lyase In Complex With A Transition Metal

The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved to 1.5A, 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 2.0A) and a trigalacturonic acid-bound substrate complex (to 2.1A) Although its fold is rare, the catalytic center 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 Bronstead base is in an alternate conformation and directly interacts with the uronate group of the substrate.
PDB ID: 2V8JDownload
MMDB ID: 59798
PDB Deposition Date: 2007/8/8
Updated in MMDB: 2007/12
Experimental Method:
x-ray diffraction
Resolution: 2.01  Å
Source Organism:
Similar Structures:
Biological Unit for 2V8J: monomeric; determined by author and by software (PQS)
Molecular Components in 2V8J
Label Count Molecule
Protein (1 molecule)
Pectate Lyase
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB