PDBsum entry 2vli

Transferase

PDB id: 2vli

Contents

Protein chains

164 a.a. *

173 a.a. *

Metals

_CL

_CD

Waters ×226

* Residue conservation analysis

PDB id:

2vli

Name:

Transferase

Title:

Structure of deinococcus radiodurans tunicamycin resistance protein

Structure:

Antibiotic resistance protein. Chain: a, b. Synonym: tunicamycin resistance protein. Engineered: yes

Source:

Deinococcus radiodurans. Organism_taxid: 243230. Strain: r1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

1.95Å R-factor: 0.176 R-free: 0.214

Authors:

S.Macedo,U.Kapp,I.Leiros,D.R.Hall,E.Mitchell

Key ref:

U.Kapp et al. (2008). Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase. Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 479-486. PubMed id: 18540055

Date:

15-Jan-08 Release date: 17-Jun-08

Protein chain

Q9RUG7  (Q9RUG7_DEIRA) -  Antibiotic resistance protein from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

Seq: 195 a.a.

Struc: 164 a.a.

Protein chain

Q9RUG7  (Q9RUG7_DEIRA) -  Antibiotic resistance protein from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

Seq: 195 a.a.

Struc: 173 a.a.

Acta Crystallogr Sect F Struct Biol Cryst Commun 64:479-486 (2008)

PubMed id: 18540055

Structure of Deinococcus radiodurans tunicamycin-resistance protein (TmrD), a phosphotransferase.

U.Kapp, S.Macedo, D.R.Hall, I.Leiros, S.M.McSweeney, E.Mitchell.

ABSTRACT

The open-reading frame (ORF) DR_1419 in the Deinococcus radiodurans genome is annotated as a representative of the wide family of tunicamycin-resistance proteins as identified in a range of bacterial genomes. The D. radiodurans ORF DR_1419 was cloned and expressed; the protein TmrD was crystallized and its X-ray crystal structure was determined to 1.95 A resolution. The structure was determined using single-wavelength anomalous diffraction with selenomethionine-derivatized protein. The refined structure is the first to be reported for a member of the tunicamycin-resistance family. It reveals strong structural similarity to the family of nucleoside monophosphate kinases and to the chloramphenicol phosphotransferase of Streptomyces venezuelae, suggesting that the mode of action is possibly by phosphorylation of tunicamycin.