PDBsum entry: 3h4t

Transferase

PDB id: 3h4t

Contents

Protein chain

390 a.a. *

Ligands

PO4 ×4

UDP

Waters ×589

* Residue conservation analysis

PDB id:

3h4t

Name:

Transferase

Title:

Chimeric glycosyltransferase for the generation of novel natural products - gtfah1 in complex with udp-2f-glc

Structure:

Glycosyltransferase gtfa, glycosyltransferase. Chain: a. Fragment: unp residues 1-214, unp residues 218-393. Synonym: gtfa, orf1, pcza361.19, gtfa protein. Engineered: yes

Source:

Amycolatopsis orientalis, actinoplanes teichomyceticus. Organism_taxid: 31958, 1867. Gene: gtfa. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.15Å R-factor: 0.170 R-free: 0.182

Authors:

M.V.B.Dias,A.W.Truman,S.Wu,T.L.Blundell,F.Huang,J.B.Spencer

Key ref:

A.W.Truman et al. (2009). Chimeric glycosyltransferases for the generation of hybrid glycopeptides. Chem Biol, 16, 676-685. PubMed id: 19549605 DOI: 10.1016/j.chembiol.2009.04.013

Date:

20-Apr-09 Release date: 28-Jul-09

Protein chain

P96558  (P96558_AMYOR) -  Glycosyltransferase GtfA

Seq: 396 a.a.

Struc: 390 a.a.*

Protein chain

Q6ZZJ7  (Q6ZZJ7_ACTTI) -  Glycosyltransferase

Seq: 393 a.a.

Struc: 390 a.a.*

* PDB and UniProt seqs differ at 139 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Biological process: metabolic process (3 terms)
• Biochemical function: transferase activity (3 terms)

DOI no: 10.1016/j.chembiol.2009.04.013

Chem Biol 16:676-685 (2009)

PubMed id: 19549605

Chimeric glycosyltransferases for the generation of hybrid glycopeptides.

A.W.Truman, M.V.Dias, S.Wu, T.L.Blundell, F.Huang, J.B.Spencer.

ABSTRACT

Glycodiversification, an invaluable tool for generating biochemical diversity, can be catalyzed by glycosyltransferases, which attach activated sugar "donors" onto "acceptor" molecules. However, many glycosyltransferases can tolerate only minor modifications to their native substrates, thus making them unsuitable tools for current glycodiversification strategies. Here we report the production of functional chimeric glycosyltransferases by mixing and matching the N- and C-terminal domains of glycopeptide glycosyltransferases. Using this method we have generated hybrid glycopeptides and have demonstrated that domain swapping can result in a predictable switch of substrate specificity, illustrating that N- and C-terminal domains predominantly dictate acceptor and donor specificity, respectively. The determination of the structure of a chimera in complex with a sugar donor analog shows that almost all sugar-glycosyltransferase binding interactions occur in the C-terminal domain.