PDBsum entry 5f15

Transferase

PDB id: 5f15

Contents

Protein chain

541 a.a.

Ligands

MPG ×76

EPE

PO4

5TR

Metals

_CL ×2

Waters ×6

PDB id:

5f15

Name:

Transferase

Title:

Crystal structure of arnt from cupriavidus metallidurans bound to undecaprenyl phosphate

Structure:

4-amino-4-deoxy-l-arabinose (l-ara4n) transferase. Chain: a. Engineered: yes

Source:

Cupriavidus metallidurans (strain atcc 43123 / dsm 2839 / nbrc 102507 / ch34). Organism_taxid: 266264. Strain: atcc 43123 / dsm 2839 / nbrc 102507 / ch34. Gene: rmet_4828, amt. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

3.20Å R-factor: 0.224 R-free: 0.263

Authors:

V.I.Petrou,O.B.Clarke,D.Tomasek,S.Banerjee,K.R.Rajashankar,F.Mancia, New York Consortium On Membrane Protein Structure (Nycomps)

Key ref:

V.I.Petrou et al. (2016). Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. Science, 351, 608-612. PubMed id: 26912703

Date:

30-Nov-15 Release date: 17-Feb-16

Protein chain

Q1LDT6  (Q1LDT6_CUPMC) -  4-amino-4-deoxy-L-arabinose transferase or related glycosyltransferases of PMT family from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)

Seq: 575 a.a.

Struc: 541 a.a.

Science 351:608-612 (2016)

PubMed id: 26912703

Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation.

V.I.Petrou, C.M.Herrera, K.M.Schultz, O.B.Clarke, J.Vendome, D.Tomasek, S.Banerjee, K.R.Rajashankar, M.Belcher Dufrisne, B.Kloss, E.Kloppmann, B.Rost, C.S.Klug, M.S.Trent, L.Shapiro, F.Mancia.

ABSTRACT

Polymyxins are antibiotics used in the last line of defense to combat multidrug-resistant infections by Gram-negative bacteria. Polymyxin resistance arises through charge modification of the bacterial outer membrane with the attachment of the cationic sugar 4-amino-4-deoxy-l-arabinose to lipid A, a reaction catalyzed by the integral membrane lipid-to-lipid glycosyltransferase 4-amino-4-deoxy-L-arabinose transferase (ArnT). Here, we report crystal structures of ArnT from Cupriavidus metallidurans, alone and in complex with the lipid carrier undecaprenyl phosphate, at 2.8 and 3.2 angstrom resolution, respectively. The structures show cavities for both lipidic substrates, which converge at the active site. A structural rearrangement occurs on undecaprenyl phosphate binding, which stabilizes the active site and likely allows lipid A binding. Functional mutagenesis experiments based on these structures suggest a mechanistic model for ArnT family enzymes.