Structural characterisation of methanogen pseudomurein cell wall peptide ligases homologous to bacterial MurE/F murein peptide ligases.

Simple item page
dc.citation.issue9
dc.citation.volume168
dc.contributor.authorSubedi BP
dc.contributor.authorSchofield LR
dc.contributor.authorCarbone V
dc.contributor.authorWolf M
dc.contributor.authorMartin WF
dc.contributor.authorRonimus RS
dc.contributor.authorSutherland-Smith AJ
dc.coverage.spatialEngland
dc.date.available2022-09
dc.date.issued2022-09
dc.description.abstractArchaea have diverse cell wall types, yet none are identical to bacterial peptidoglycan (murein). Methanogens Methanobacteria and Methanopyrus possess cell walls of pseudomurein, a structural analogue of murein. Pseudomurein differs from murein in containing the unique archaeal sugar N-acetyltalosaminuronic acid instead of N-acetylmuramic acid, β-1,3 glycosidic bonds in place of β-1,4 bonds and only l-amino acids in the peptide cross-links. We have determined crystal structures of methanogen pseudomurein peptide ligases (termed pMurE) from Methanothermus fervidus (Mfer762) and Methanothermobacter thermautotrophicus (Mth734) that are structurally most closely related to bacterial MurE peptide ligases. The homology of the archaeal pMurE and bacterial MurE enzymes is clear both in the overall structure and at the level of each of the three domains. In addition, we identified two UDP-binding sites in Mfer762 pMurE, one at the exterior surface of the interface of the N-terminal and middle domains, and a second site at an inner surface continuous with the highly conserved interface of the three domains. Residues involved in ATP binding in MurE are conserved in pMurE, suggesting that a similar ATP-binding pocket is present at the interface of the middle and the C-terminal domains of pMurE. The presence of pMurE ligases in members of the Methanobacteriales and Methanopyrales, that are structurally related to bacterial MurE ligases, supports the idea that the biosynthetic origins of archaeal pseudomurein and bacterial peptidoglycan cell walls are evolutionarily related.
dc.description.publication-statusPublished
dc.identifierhttps://www.ncbi.nlm.nih.gov/pubmed/36178458
dc.identifier.citationMicrobiology (Reading), 2022, 168 (9)
dc.identifier.doi10.1099/mic.0.001235
dc.identifier.eissn1465-2080
dc.identifier.elements-id457152
dc.identifier.harvestedMassey_Dark
dc.identifier.urihttps://hdl.handle.net/10179/18009
dc.languageeng
dc.relation.isPartOfMicrobiology (Reading)
dc.subjectMurE
dc.subjectmethanogen
dc.subjectmurein
dc.subjectpMurE
dc.subjectpeptide ligase
dc.subjectpseudomurein
dc.subjectAdenosine Triphosphate
dc.subjectAmino Acids
dc.subjectArchaea
dc.subjectBacteria
dc.subjectCell Wall
dc.subjectEuryarchaeota
dc.subjectLigases
dc.subjectPeptide Synthases
dc.subjectPeptidoglycan
dc.subjectSugars
dc.subjectUridine Diphosphate
dc.titleStructural characterisation of methanogen pseudomurein cell wall peptide ligases homologous to bacterial MurE/F murein peptide ligases.
dc.typeJournal article
pubs.notesNot known
pubs.organisational-group/Massey University
pubs.organisational-group/Massey University/College of Sciences
pubs.organisational-group/Massey University/College of Sciences/School of Natural Sciences
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Subedi-2022.pdf
Size:
6.43 MB
Format:
Adobe Portable Document Format
Description:
Download
Collections
Journal Articles