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TitleNlpC/P60 peptidoglycan hydrolases of Trichomonas vaginalis have complementary activities that empower the protozoan to control host-protective lactobacilli.
Journal, issue, pagesPlos Pathog., Vol. 19, Page e1011563-e1011563, Year 2023
Publish dateOct 19, 2022 (structure data deposition date)
AuthorsBarnett, M.J. / Pinheiro, J. / Keown, J.R. / Biboy, J. / Gray, J. / Lucinescu, I.W. / Vollmer, W. / Hirt, R.P. / Simoes-Barbosa, A. / Goldstone, D.C.
External linksPlos Pathog. / PubMed:37585473
MethodsX-ray diffraction
Resolution1.3 - 1.65 Å
Structure data

PDB-8ev4:
NlpC B3 - Trichomonas Vaginalis
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-8ev5:
NlpC B3 covalently bound with E64 inhibitor fragment
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-E64:
N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE

ChemComp-SO4:
SULFATE ION

Source
  • trichomonas vaginalis g3 (eukaryote)
  • trichomonas vaginalis (eukaryote)
KeywordsHYDROLASE / NlpC / P60 / CHAP / NlpC/P60 / Cysteine Protease / HYDROLASE/Inhibitor / inhibitor / E64 / HYDROLASE-Inhibitor complex

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