Structure of the diaminopimelate epimerase DapF from  Mycobacterium tuberculosis

V Usha; LG Dover; DI Roper; Klaus Futterer; Gurdyal Besra

doi:10.1107/S0907444909002522

Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis

V Usha, LG Dover, DI Roper, Klaus Futterer, Gurdyal Besra

Biosciences

Research output: Contribution to journal › Article

16 Citations (Scopus)

Abstract

The meso (or d,L) isomer of diaminopimelic acid (DAP), a precursor of L-lysine, is a key component of the pentapeptide linker in bacterial peptidoglycan. While the peptidoglycan incorporated in the highly complex cell wall of the pathogen Mycobacterium tuberculosis structurally resembles that of Escherichia coli, it is unique in that it can contain penicillin-resistant meso-DAP -> meso-DAP linkages. The interconversion of L,L-DAP and meso-DAP is catalysed by the DAP epimerase DapF, a gene product that is essential in M. tuberculosis. Here, the crystal structure of the ligand-free form of M. tuberculosis DapF (MtDapF) refined to a resolution of 2.6 angstrom is reported. MtDapF shows small if distinct deviations in secondary structure from the two-domain alpha/beta-fold of the known structures of Haemophilus influenzae DapF and Bacillus anthracis DapF, which are in line with its low sequence identity (

Original language	English
Pages (from-to)	383-387
Number of pages	5
Journal	Acta Crystallographica Section D Biological Crystallography
Volume	65
Issue number	4
DOIs	https://doi.org/10.1107/S0907444909002522
Publication status	Published - 1 Apr 2009

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1107/S0907444909002522

MAGPIE Project: The Structure and Assembly of the Mycobacterial Cell Envelope
Besra, D., Lammas, T. & Minnikin, D.
Medical Research Council
1/02/06 → 31/01/11
Project: Research Councils

Cite this

@article{845dad2aa39b4bbf86943230eabd7bab,

title = "Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis",

abstract = "The meso (or d,L) isomer of diaminopimelic acid (DAP), a precursor of L-lysine, is a key component of the pentapeptide linker in bacterial peptidoglycan. While the peptidoglycan incorporated in the highly complex cell wall of the pathogen Mycobacterium tuberculosis structurally resembles that of Escherichia coli, it is unique in that it can contain penicillin-resistant meso-DAP -> meso-DAP linkages. The interconversion of L,L-DAP and meso-DAP is catalysed by the DAP epimerase DapF, a gene product that is essential in M. tuberculosis. Here, the crystal structure of the ligand-free form of M. tuberculosis DapF (MtDapF) refined to a resolution of 2.6 angstrom is reported. MtDapF shows small if distinct deviations in secondary structure from the two-domain alpha/beta-fold of the known structures of Haemophilus influenzae DapF and Bacillus anthracis DapF, which are in line with its low sequence identity (",

author = "V Usha and LG Dover and DI Roper and Klaus Futterer and Gurdyal Besra",

year = "2009",

month = apr,

day = "1",

doi = "10.1107/S0907444909002522",

language = "English",

volume = "65",

pages = "383--387",

journal = "Acta Crystallographica Section D Biological Crystallography",

publisher = "International Union of Crystallography",

number = "4",

}

TY - JOUR

T1 - Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis

AU - Usha, V

AU - Dover, LG

AU - Roper, DI

AU - Futterer, Klaus

AU - Besra, Gurdyal

PY - 2009/4/1

Y1 - 2009/4/1

N2 - The meso (or d,L) isomer of diaminopimelic acid (DAP), a precursor of L-lysine, is a key component of the pentapeptide linker in bacterial peptidoglycan. While the peptidoglycan incorporated in the highly complex cell wall of the pathogen Mycobacterium tuberculosis structurally resembles that of Escherichia coli, it is unique in that it can contain penicillin-resistant meso-DAP -> meso-DAP linkages. The interconversion of L,L-DAP and meso-DAP is catalysed by the DAP epimerase DapF, a gene product that is essential in M. tuberculosis. Here, the crystal structure of the ligand-free form of M. tuberculosis DapF (MtDapF) refined to a resolution of 2.6 angstrom is reported. MtDapF shows small if distinct deviations in secondary structure from the two-domain alpha/beta-fold of the known structures of Haemophilus influenzae DapF and Bacillus anthracis DapF, which are in line with its low sequence identity (

AB - The meso (or d,L) isomer of diaminopimelic acid (DAP), a precursor of L-lysine, is a key component of the pentapeptide linker in bacterial peptidoglycan. While the peptidoglycan incorporated in the highly complex cell wall of the pathogen Mycobacterium tuberculosis structurally resembles that of Escherichia coli, it is unique in that it can contain penicillin-resistant meso-DAP -> meso-DAP linkages. The interconversion of L,L-DAP and meso-DAP is catalysed by the DAP epimerase DapF, a gene product that is essential in M. tuberculosis. Here, the crystal structure of the ligand-free form of M. tuberculosis DapF (MtDapF) refined to a resolution of 2.6 angstrom is reported. MtDapF shows small if distinct deviations in secondary structure from the two-domain alpha/beta-fold of the known structures of Haemophilus influenzae DapF and Bacillus anthracis DapF, which are in line with its low sequence identity (

U2 - 10.1107/S0907444909002522

DO - 10.1107/S0907444909002522

M3 - Article

C2 - 19307721

VL - 65

SP - 383

EP - 387

JO - Acta Crystallographica Section D Biological Crystallography

JF - Acta Crystallographica Section D Biological Crystallography

IS - 4

ER -

Structure of the diaminopimelate epimerase DapF from Mycobacterium tuberculosis

Abstract

UN SDGs

Access to Document

Fingerprint

Projects

MAGPIE Project: The Structure and Assembly of the Mycobacterial Cell Envelope

Cite this