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http://purl.uniprot.org/citations/22569035http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22569035http://www.w3.org/2000/01/rdf-schema#comment"Aspergilloglutamic peptidase from Aspergillus niger var. macrosporus (AGP) is one of the so-called pepstatin-insensitive acid endopeptidases, which are distinct from the well-studied aspartic peptidases. Among the known homologues of the glutamic peptidases, AGP is a unique two-chain enzyme with a light chain and a heavy chain bound non-covalently with each other, and thus is an interesting target for protein structure-function relationship studies. In this article, we report the crystal structure of a dimeric form of the enzyme at a resolution of 1.6 Å. This form has a unique structure in which the C-terminal region of the light chain of one of the molecules binds to the active site cleft of the other molecule like a part of a substrate. This form mimics the enzyme-activation product complex produced upon autoproteolysis, and provides a structural clue that could help to clarify the activation mechanism. This type of dimeric structure of a peptidase is here reported for the first time."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.org/dc/terms/identifier"doi:10.1093/jb/mvs050"xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Kubota K."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Kojima M."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Nakagawa A."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Lee W.C."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Takahashi K."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Iwata S."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Tanokura M."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Sasaki H."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/author"Ohtsuka J."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/name"J Biochem"xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/pages"45-52"xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/title"The crystal structure of an intermediate dimer of aspergilloglutamic peptidase that mimics the enzyme-activation product complex produced upon autoproteolysis."xsd:string
http://purl.uniprot.org/citations/22569035http://purl.uniprot.org/core/volume"152"xsd:string
http://purl.uniprot.org/citations/22569035http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22569035
http://purl.uniprot.org/citations/22569035http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22569035
http://purl.uniprot.org/uniprot/#_P24665-mappedCitation-22569035http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22569035
http://purl.uniprot.org/uniprot/P24665http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22569035