Entry Database : PDB / ID : 7tj4 Structure visualization Downloads & linksTitle Structure of the S. aureus amidase LytH and activator ActH extracellular domains Components Details Keywords HYDROLASE / amidaseFunction / homology Function and homology informationFunction Domain/homology Component
rhomboid protease / N-acetylmuramoyl-L-alanine amidase activity / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / peptidoglycan catabolic process / cell wall organization / membrane => GO:0016020 / serine-type endopeptidase activity / extracellular region Similarity search - Function Probable cell wall amidase LytH / Bacterial SH3 domain / Ami_3 / N-acetylmuramoyl-L-alanine amidase, catalytic domain / N-acetylmuramoyl-L-alanine amidase / SH3b domain profile. / Bacterial SH3 domain homologues / SH3-like domain, bacterial-type / Peptidase S54, rhomboid domain / Rhomboid family ... Probable cell wall amidase LytH / Bacterial SH3 domain / Ami_3 / N-acetylmuramoyl-L-alanine amidase, catalytic domain / N-acetylmuramoyl-L-alanine amidase / SH3b domain profile. / Bacterial SH3 domain homologues / SH3-like domain, bacterial-type / Peptidase S54, rhomboid domain / Rhomboid family / Rhomboid-like superfamily / TPR repeat profile. / Tetratricopeptide repeat / Tetratricopeptide-like helical domain superfamily Similarity search - Domain/homologyBiological species Staphylococcus aureus (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution : 1.8 Å DetailsAuthors Page, J.E. / Skiba, M.A. / Kruse, A.C. / Walker, S. Funding support United States, 4items Details Hide detailsOrganization Grant number Country National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) R01 AI139011 United States National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) R01 AI148752 United States National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) T32 GM007753 United States National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) F30 AI156972 United States
CitationJournal : Proc.Natl.Acad.Sci.USA / Year : 2022Title : Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Authors : Page, J.E. / Skiba, M.A. / Do, T. / Kruse, A.C. / Walker, S. History Deposition Jan 14, 2022 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Jul 6, 2022 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2022 Group : Database references / Category : citationItem : _citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.titleRevision 1.2 Jul 20, 2022 Group : Database references / Category : citation / citation_authorItem : _citation.page_first / _citation.page_last / _citation_author.identifier_ORCIDRevision 1.3 Oct 18, 2023 Group : Data collection / Refinement descriptionCategory : chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
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