PDBsum entry: 2p56

Transferase

PDB id: 2p56

Contents

Protein chain

257 a.a. *

Ligands

EDO ×5

Waters ×84

* Residue conservation analysis

PDB id:

2p56

Name:

Transferase

Title:

Crystal structure of alpha-2,3-sialyltransferase from campyl jejuni in apo form

Structure:

Alpha-2,3-sialyltransferase. Chain: a. Engineered: yes

Source:

Campylobacter jejuni. Organism_taxid: 197. Gene: cst-i. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.212 R-free: 0.250

Authors:

C.P.Chiu,L.L.Lairson,M.Gilbert,W.W.Wakarchuk,S.G.Withers, N.C.Strynadka

Key ref:

C.P.Chiu et al. (2007). Structural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms. Biochemistry, 46, 7196-7204. PubMed id: 17518445 DOI: 10.1021/bi602543d

Date:

14-Mar-07 Release date: 10-Jul-07

Protein chain

Q9RGF1  (Q9RGF1_CAMJE) -  Alpha-2,3-sialyltransferase

Seq: 430 a.a.

Struc: 257 a.a.

DOI no: 10.1021/bi602543d

Biochemistry 46:7196-7204 (2007)

PubMed id: 17518445

Structural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms.

C.P.Chiu, L.L.Lairson, M.Gilbert, W.W.Wakarchuk, S.G.Withers, N.C.Strynadka.

ABSTRACT

Sialic acid is an essential sugar in biology that plays key roles in numerous cellular processes and interactions. The biosynthesis of sialylated glycoconjugates is catalyzed by five distinct families of sialyltransferases. In the last 25 years, there has been much research on the enzymes themselves, their genes, and their reaction products, but we still do not know the precise molecular mechanism of action for this class of glycosyltransferase. We previously reported the first detailed structural and kinetic characterization of Cst-II, a bifunctional sialyltransferase (CAZy GT-42) from the bacterium Campylobacter jejuni [Chiu et al. (2004) Nat. Struct. Mol. Biol. 11, 163-170]. This enzyme can use both Gal-beta-1,3/4-R and Neu5Ac-alpha-2,3-Gal-beta-1,3/4-R as acceptor sugars. A second sialyltransferase from this bacterium, Cst-I, has been shown to utilize solely Gal-beta-1,3/4-R as the acceptor sugar in its transferase reaction. We report here the structural and kinetic characterization of this monofunctional enzyme, which belongs to the same sialyltransferase family as Cst-II, in both apo and substrate bound form. Our structural data show that Cst-I adopts a similar GTA-type glycosyltransferase fold to that of the bifunctional Cst-II, with conservation of several key noncharged catalytic residues. Significant differences are found, however, between the two enzymes in the lid domain region, which is critical to the creation of the acceptor sugar binding site. Furthermore, molecular modeling of various acceptor sugars within the active sites of these enzymes provides significant new insights into the structural basis for substrate specificities within this biologically important enzyme class.