PDBsum entry: 3h4i

Transferase

PDB-id: 3h4i

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Description

Header details

Header records

References

PROCHECK

Protein chain

392 a.a. *

Ligands

U2F

SO4 ×2

Waters ×630

* Residue conservation analysis

Tools

Clefts Calculation

• PDB id: 3h4i
• Name: Transferase
• Title: Chimeric glycosyltransferase for the generation of novel natural products
• 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.

UniProt:

()

()

• Resolution: 1.30Å
• R-factor: 0.165
• R-free: 0.184
• 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
• Related entries: 3h4t ; the same protein complexed with udp

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Clefts

Surface

Key reference

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.