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NlpI scaffolds hydrolases within peptidoglycan multi-enzyme complexes in Escherichia coli

ABSTRACT: We performed enrichment of nlpI to study its function in Escherichia coli.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Escherichia Coli

SUBMITTER: Frank Stein

LAB HEAD: Athanasios Typas

PROVIDER: PXD016825 | Pride | 2020-02-25

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	140814_ZB_Manu_E1_Ctrl.raw	Raw
	140814_ZB_Manu_E1_Nlpl.raw	Raw
	140814_ZB_Manu_E1_dC11.raw	Raw
	140814_ZB_Manu_HE1_Ctrl.raw	Raw
	140814_ZB_Manu_HE1_Nlpl.raw	Raw

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1 - 5 of 17

Publications

Outer membrane lipoprotein NlpI scaffolds peptidoglycan hydrolases within multi-enzyme complexes in Escherichia coli.

Banzhaf Manuel M Yau Hamish Cl HC Verheul Jolanda J Lodge Adam A Kritikos George G Mateus André A Cordier Baptiste B Hov Ann Kristin AK Stein Frank F Wartel Morgane M Pazos Manuel M Solovyova Alexandra S AS Breukink Eefjan E van Teeffelen Sven S Savitski Mikhail M MM den Blaauwen Tanneke T Typas Athanasios A Vollmer Waldemar W

The EMBO journal 20200203 5

The peptidoglycan (PG) sacculus provides bacteria with the mechanical strength to maintain cell shape and resist osmotic stress. Enlargement of the mesh-like sacculus requires the combined activity of peptidoglycan synthases and hydrolases. In Escherichia coli, the activity of two PG synthases is driven by lipoproteins anchored in the outer membrane (OM). However, the regulation of PG hydrolases is less well understood, with only regulators for PG amidases having been described. Here, we identif ...[more]

PMID: 32009249

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