2v8k
From Proteopedia
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STRUCTURE OF A FAMILY 2 PECTATE LYASE IN COMPLEX WITH TRIGALACTURONIC ACID
Overview
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.
About this Structure
2V8K is a Single protein structure of sequence from Yersinia enterocolitica with as ligand. Active as Pectate lyase, with EC number 4.2.2.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
A Family 2 Pectate Lyase Displays a Rare Fold and Transition Metal-assisted -Elimination., Abbott DW, Boraston AB, J Biol Chem. 2007 Nov 30;282(48):35328-36. Epub 2007 Sep 19. PMID:17881361
Page seeded by OCA on Sun Feb 3 10:50:29 2008
