PDBsum entry 2jzc

Transferase

PDB id: 2jzc

Contents

Protein chain

201 a.a. *

* Residue conservation analysis

PDB id:

2jzc

Name:

Transferase

Title:

Nmr solution structure of alg13: the sugar donor subunit of a yeast n- acetylglucosamine transferase. Northeast structural genomics consortium target yg1

Structure:

Udp-n-acetylglucosamine transferase subunit alg13. Chain: a. Synonym: asparagine-linked glycosylation protein 13. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: s288c. Atcc: 204508. Gene: alg13, ygl047w. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

10 models

Authors:

X.Wang,T.Weldeghorghis,G.Zhang,B.Imepriali,G.T.Montelione, J.H.Prestegard,Northeast Structural Genomics Consortium (Nesg)

Key ref:

X.Wang et al. (2008). Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase. Structure, 16, 965-975. PubMed id: 18547528 DOI: 10.1016/j.str.2008.03.010

Date:

04-Jan-08 Release date: 19-Feb-08

Protein chain

P53178  (ALG13_YEAST) -  UDP-N-acetylglucosamine transferase subunit ALG13 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 202 a.a.

Struc: 201 a.a.

Enzyme reactions

• Enzyme class: E.C.2.4.1.141 - N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase.
• Reaction: an N-acetyl-alpha-D-glucosaminyl-diphospho-di-trans,poly-cis-dolichol + UDP-N-acetyl-alpha-D-glucosamine = an N,N'-diacetylchitobiosyl-diphospho- di-trans,poly-cis-dolichol + UDP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Key reference

DOI no: 10.1016/j.str.2008.03.010

Structure 16:965-975 (2008)

PubMed id: 18547528

Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase.

X.Wang, T.Weldeghiorghis, G.Zhang, B.Imperiali, J.H.Prestegard.

ABSTRACT

The solution structure of Alg13, the glycosyl donor-binding domain of an important bipartite glycosyltransferase in the yeast Saccharomyces cerevisiae, is presented. This glycosyltransferase is unusual in that it is active only in the presence of a binding partner, Alg14. Alg13 is found to adopt a unique topology among glycosyltransferases. Rather than the conventional Rossmann fold found in all GT-B enzymes, the N-terminal half of the protein is a Rossmann-like fold with a mixed parallel and antiparallel beta sheet. The Rossmann fold of the C-terminal half of Alg13 is conserved. However, although conventional GT-B enzymes usually possess three helices at the C terminus, only two helices are present in Alg13. Titration of Alg13 with both UDP-GlcNAc, the native glycosyl donor, and a paramagnetic mimic, UDP-TEMPO, shows that the interaction of Alg13 with the sugar donor is primarily through the residues in the C-terminal half of the protein.

Selected figure(s)

Figure 2.
Figure 2. Annotated HSQC Spectrum of Deuterated Alg13
Each assigned peak is labeled with the residue number and one letter residue name.

Figure 4.
Figure 4. Topology Representations of Alg 13
(A) Schematic illustration of the predicted topology of Alg13. The numbering of the element is according to the scheme from Figure 1. Note that the predicted helix after β2 gave rise to both α3 and β3.
(B) Schematic illustration of the experimentally determined topology of Alg13.

The above figures are reprinted from an Open Access publication published by Cell Press: Structure (2008, 16, 965-975) copyright 2008.

Figures were selected by an automated process.