000095792 001__ 95792
000095792 005__ 20250731113508.0
000095792 0247_ $$2pmid$$apmid:20223213
000095792 0247_ $$2doi$$a10.1016/j.str.2010.01.005
000095792 0247_ $$2ISSN$$a0969-2126
000095792 0247_ $$2ISSN$$a1878-4186
000095792 0247_ $$2WOS$$aWOS:000275492000007
000095792 0247_ $$2openalex$$aopenalex:W2099183713
000095792 037__ $$aPHPPUBDB-19255
000095792 041__ $$aeng
000095792 082__ $$a570
000095792 1001_ $$aBokhove, M.
000095792 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000095792 245__ $$aStructures of an isopenicillin N converting Ntn-hydrolase reveal different catalytic roles for the active site residues of precursor and mature enzyme.
000095792 260__ $$aLondon [u.a.]$$bElsevier Science$$c2010
000095792 300__ $$a301-308
000095792 3367_ $$00$$2EndNote$$aJournal Article
000095792 3367_ $$2BibTeX$$aARTICLE
000095792 3367_ $$2DRIVER$$aarticle
000095792 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$mjournal
000095792 440_0 $$0PERI:(DE-600)2031189-8$$aStructure$$v18$$x0969-2126
000095792 500__ $$3Converted on 2013-05-30 15:23
000095792 500__ $$3Converted on 2013-06-21 19:21
000095792 520__ $$aPenicillium chrysogenum Acyl coenzyme A:isopenicillin N acyltransferase (AT) performs the last step in the biosynthesis of hydrophobic penicillins, exchanging the hydrophilic side chain of a precursor for various hydrophobic side chains. Like other N-terminal nucleophile hydrolases AT is produced as an inactive precursor that matures upon posttranslational cleavage. The structure of a Cys103Ala precursor mutant shows that maturation is autoproteolytic, initiated by Cys103 cleaving its preceding peptide bond. The crystal structure of the mature enzyme shows that after autoproteolysis residues 92-102 fold outwards, exposing a buried pocket. This pocket is structurally and chemically flexible and can accommodate substrates of different size and polarity. Modeling of a substrate-bound state indicates the residues important for catalysis. Comparison of the proposed autoproteolytic and substrate hydrolysis mechanisms shows that in both events the same catalytic residues are used, but that they perform different roles in catalysis.
000095792 536__ $$0G:(DE-H253)POF2-BW7-20130405$$aDORIS Beamline BW7 (POF2-54G13)$$cPOF2-54G13$$fPOF II$$x0
000095792 588__ $$aDataset connected to Pubmed
000095792 650_2 $$2MeSH$$aAcyltransferases: chemistry
000095792 650_2 $$2MeSH$$aAcyltransferases: metabolism
000095792 650_2 $$2MeSH$$aAmidohydrolases: chemistry
000095792 650_2 $$2MeSH$$aAmidohydrolases: metabolism
000095792 650_2 $$2MeSH$$aCatalysis
000095792 650_2 $$2MeSH$$aCatalytic Domain
000095792 650_2 $$2MeSH$$aCrystallography, X-Ray
000095792 650_2 $$2MeSH$$aCysteine: chemistry
000095792 650_2 $$2MeSH$$aCysteine: metabolism
000095792 650_2 $$2MeSH$$aHydrolysis
000095792 650_2 $$2MeSH$$aModels, Molecular
000095792 650_2 $$2MeSH$$aPenicillin-Binding Proteins: chemistry
000095792 650_2 $$2MeSH$$aPenicillin-Binding Proteins: metabolism
000095792 650_2 $$2MeSH$$aPenicillins: chemistry
000095792 650_2 $$2MeSH$$aPenicillins: metabolism
000095792 650_2 $$2MeSH$$aProtein Conformation
000095792 650_7 $$00$$2NLM Chemicals$$aPenicillin-Binding Proteins
000095792 650_7 $$00$$2NLM Chemicals$$aPenicillins
000095792 650_7 $$052-90-4$$2NLM Chemicals$$aCysteine
000095792 650_7 $$0EC 2.3.-$$2NLM Chemicals$$aAcyltransferases
000095792 650_7 $$0EC 2.3.1.-$$2NLM Chemicals$$aacyl-CoA-6-aminopenicillanic acid acyltransferase
000095792 650_7 $$0EC 3.5.-$$2NLM Chemicals$$aAmidohydrolases
000095792 650_7 $$0EC 3.5.1.-$$2NLM Chemicals$$aN-terminal nucleophile hydrolase
000095792 650_7 $$0NOF9U9EYQ4$$2NLM Chemicals$$apenicillin N
000095792 693__ $$0EXP:(DE-H253)D-BW7-20150101$$1EXP:(DE-H253)DORISIII-20150101$$6EXP:(DE-H253)D-BW7-20150101$$aDORIS III$$fDORIS Beamline BW7$$x0
000095792 7001_ $$aYoshida, H.
000095792 7001_ $$aHensgens, C. M. H.
000095792 7001_ $$avan der Laan, J. M.
000095792 7001_ $$aSutherland, J. D.
000095792 7001_ $$aDijkstra, B. W.
000095792 773__ $$0PERI:(DE-600)2031189-8$$a10.1016/j.str.2010.01.005$$gVol. 18, p. 301-308$$p301-308$$q18<301-308$$tStructure$$v18$$x0969-2126$$y2010
000095792 85640 $$uhttp://www.ncbi.nlm.nih.gov/pubmed/20223213
000095792 909CO $$ooai:bib-pubdb1.desy.de:95792$$pVDB
000095792 9101_ $$0I:(DE-HGF)0$$aExternes Institut$$kExtern
000095792 9131_ $$0G:(DE-HGF)POF2-54G13$$1G:(DE-HGF)POF2-540$$2G:(DE-HGF)POF2-500$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$9G:(DE-H253)POF2-BW7-20130405$$aDE-H253$$bStruktur der Materie$$lForschung mit Photonen, Neutronen, Ionen$$vDORIS III$$x0
000095792 9141_ $$y2010
000095792 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aMedline
000095792 915__ $$0StatID:(DE-HGF)1$$2StatID$$aNo Author Disambiguation
000095792 920_1 $$iEuropean Molecular Biology Laboratory$$kEMBL
000095792 9201_ $$0I:(DE-H253)EMBL_-2012_-20130307$$kEMBL$$lEuropean Molecular Biology Laboratory$$x0
000095792 920__ $$k001
000095792 980__ $$aPHPPUBDB
000095792 980__ $$aVDB
000095792 980__ $$aUNRESTRICTED
000095792 980__ $$ajournal
000095792 980__ $$aI:(DE-H253)EMBL_-2012_-20130307
000095792 980__ $$aConvertedRecord