Three-dimensional structure of the bacterial cell wall peptidoglycan

Samy Meroueh, Krisztina Z. Bencze, Dusan Hesek, Mijoon Lee, Jed F. Fisher, Timothy L. Stemmler, Shahriar Mobashery

Research output: Contribution to journalArticle

226 Citations (Scopus)

Abstract

The 3D structure of the bacterial peptidoglycan, the major constituent of the cell wall, is one of the most important, yet still unsolved, structural problems in biochemistry. The peptidoglycan comprises alternating N-acetylglucosamine (NAG) and N-acetylmuramic disaccharide (NAM) saccharides, the latter of which has a peptide stem. Adjacent peptide stems are cross-linked by the transpeptidase enzymes of cell wall biosynthesis to provide the cell wall polymer with the structural integrity required by the bacterium. The cell wall and its biosynthetic enzymes are targets of antibiotics. The 3D structure of the cell wall has been elusive because of its complexity and the lack of pure samples. Herein we report the 3D solution structure as determined by NMR of the 2-kDa NAG-NAM(pentapeptide)-NAG-NAM(pentapeptide) synthetic fragment of the cell wall. The glycan backbone of this peptidoglycan forms a right-handed helix with a periodicity of three for the NAG-NAM repeat (per turn of the helix). The first two amino acids of the pentapeptide adopt a limited number of conformations. Based on this structure a model for the bacterial cell wall is proposed.

Original languageEnglish (US)
Pages (from-to)4404-4409
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume103
Issue number12
DOIs
StatePublished - Mar 21 2006
Externally publishedYes

Fingerprint

Bacterial Structures
Peptidoglycan
Cell Wall
Acetylglucosamine
Disaccharides
Peptidyl Transferases
Artificial Cells
Peptides
Periodicity
Enzymes
Biochemistry
Polysaccharides
Polymers
Anti-Bacterial Agents
Bacteria
Amino Acids

Keywords

  • Bacterial envelope
  • Murein sacculus

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Three-dimensional structure of the bacterial cell wall peptidoglycan. / Meroueh, Samy; Bencze, Krisztina Z.; Hesek, Dusan; Lee, Mijoon; Fisher, Jed F.; Stemmler, Timothy L.; Mobashery, Shahriar.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 103, No. 12, 21.03.2006, p. 4404-4409.

Research output: Contribution to journalArticle

Meroueh, Samy ; Bencze, Krisztina Z. ; Hesek, Dusan ; Lee, Mijoon ; Fisher, Jed F. ; Stemmler, Timothy L. ; Mobashery, Shahriar. / Three-dimensional structure of the bacterial cell wall peptidoglycan. In: Proceedings of the National Academy of Sciences of the United States of America. 2006 ; Vol. 103, No. 12. pp. 4404-4409.
@article{298d08c4b9bf47adb554d8e1a0239be1,
title = "Three-dimensional structure of the bacterial cell wall peptidoglycan",
abstract = "The 3D structure of the bacterial peptidoglycan, the major constituent of the cell wall, is one of the most important, yet still unsolved, structural problems in biochemistry. The peptidoglycan comprises alternating N-acetylglucosamine (NAG) and N-acetylmuramic disaccharide (NAM) saccharides, the latter of which has a peptide stem. Adjacent peptide stems are cross-linked by the transpeptidase enzymes of cell wall biosynthesis to provide the cell wall polymer with the structural integrity required by the bacterium. The cell wall and its biosynthetic enzymes are targets of antibiotics. The 3D structure of the cell wall has been elusive because of its complexity and the lack of pure samples. Herein we report the 3D solution structure as determined by NMR of the 2-kDa NAG-NAM(pentapeptide)-NAG-NAM(pentapeptide) synthetic fragment of the cell wall. The glycan backbone of this peptidoglycan forms a right-handed helix with a periodicity of three for the NAG-NAM repeat (per turn of the helix). The first two amino acids of the pentapeptide adopt a limited number of conformations. Based on this structure a model for the bacterial cell wall is proposed.",
keywords = "Bacterial envelope, Murein sacculus",
author = "Samy Meroueh and Bencze, {Krisztina Z.} and Dusan Hesek and Mijoon Lee and Fisher, {Jed F.} and Stemmler, {Timothy L.} and Shahriar Mobashery",
year = "2006",
month = "3",
day = "21",
doi = "10.1073/pnas.0510182103",
language = "English (US)",
volume = "103",
pages = "4404--4409",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "12",

}

TY - JOUR

T1 - Three-dimensional structure of the bacterial cell wall peptidoglycan

AU - Meroueh, Samy

AU - Bencze, Krisztina Z.

AU - Hesek, Dusan

AU - Lee, Mijoon

AU - Fisher, Jed F.

AU - Stemmler, Timothy L.

AU - Mobashery, Shahriar

PY - 2006/3/21

Y1 - 2006/3/21

N2 - The 3D structure of the bacterial peptidoglycan, the major constituent of the cell wall, is one of the most important, yet still unsolved, structural problems in biochemistry. The peptidoglycan comprises alternating N-acetylglucosamine (NAG) and N-acetylmuramic disaccharide (NAM) saccharides, the latter of which has a peptide stem. Adjacent peptide stems are cross-linked by the transpeptidase enzymes of cell wall biosynthesis to provide the cell wall polymer with the structural integrity required by the bacterium. The cell wall and its biosynthetic enzymes are targets of antibiotics. The 3D structure of the cell wall has been elusive because of its complexity and the lack of pure samples. Herein we report the 3D solution structure as determined by NMR of the 2-kDa NAG-NAM(pentapeptide)-NAG-NAM(pentapeptide) synthetic fragment of the cell wall. The glycan backbone of this peptidoglycan forms a right-handed helix with a periodicity of three for the NAG-NAM repeat (per turn of the helix). The first two amino acids of the pentapeptide adopt a limited number of conformations. Based on this structure a model for the bacterial cell wall is proposed.

AB - The 3D structure of the bacterial peptidoglycan, the major constituent of the cell wall, is one of the most important, yet still unsolved, structural problems in biochemistry. The peptidoglycan comprises alternating N-acetylglucosamine (NAG) and N-acetylmuramic disaccharide (NAM) saccharides, the latter of which has a peptide stem. Adjacent peptide stems are cross-linked by the transpeptidase enzymes of cell wall biosynthesis to provide the cell wall polymer with the structural integrity required by the bacterium. The cell wall and its biosynthetic enzymes are targets of antibiotics. The 3D structure of the cell wall has been elusive because of its complexity and the lack of pure samples. Herein we report the 3D solution structure as determined by NMR of the 2-kDa NAG-NAM(pentapeptide)-NAG-NAM(pentapeptide) synthetic fragment of the cell wall. The glycan backbone of this peptidoglycan forms a right-handed helix with a periodicity of three for the NAG-NAM repeat (per turn of the helix). The first two amino acids of the pentapeptide adopt a limited number of conformations. Based on this structure a model for the bacterial cell wall is proposed.

KW - Bacterial envelope

KW - Murein sacculus

UR - http://www.scopus.com/inward/record.url?scp=33645240931&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33645240931&partnerID=8YFLogxK

U2 - 10.1073/pnas.0510182103

DO - 10.1073/pnas.0510182103

M3 - Article

C2 - 16537437

AN - SCOPUS:33645240931

VL - 103

SP - 4404

EP - 4409

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 12

ER -