2v8k
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The family 2 pectate lyase from Yersinia enterocolitica (YePL2A), solved | + | 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== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | A | + | A family 2 pectate lyase displays a rare fold and transition metal-assisted beta-elimination., Abbott DW, Boraston AB, J Biol Chem. 2007 Nov 30;282(48):35328-36. Epub 2007 Sep 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17881361 17881361] |
[[Category: Pectate lyase]] | [[Category: Pectate lyase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia enterocolitica]] | [[Category: Yersinia enterocolitica]] | ||
| - | [[Category: Abbott, D | + | [[Category: Abbott, D W.]] |
| - | [[Category: Boraston, A | + | [[Category: Boraston, A B.]] |
[[Category: TGU]] | [[Category: TGU]] | ||
[[Category: beta-elimination]] | [[Category: beta-elimination]] | ||
| Line 23: | Line 23: | ||
[[Category: periplasm]] | [[Category: periplasm]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:01 2008'' |
Revision as of 16:54, 21 February 2008
|
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 beta-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 Thu Feb 21 18:54:01 2008
