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dc.rights.licenseopenen_US
dc.contributor.authorHARIJAN, Rajesh K
dc.contributor.authorKIEMA, Tiila-Riikka
dc.contributor.authorSYED, Shahan M
dc.contributor.authorQADIR, Imran
hal.structure.identifierCentre de résonance magnétique des systèmes biologiques [CRMSB]
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorMAZET, Muriel
hal.structure.identifierCentre de résonance magnétique des systèmes biologiques [CRMSB]
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorBRINGAUD, Frederic
dc.contributor.authorMICHELS, Paul A M
dc.contributor.authorWIERENGA, Rik K
dc.date.accessioned2023-11-03T16:35:58Z
dc.date.available2023-11-03T16:35:58Z
dc.date.issued2017-03-01
dc.identifier.issn1741-0134en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/184591
dc.description.abstractEnStructures of the C123A variant of the dimeric Leishmania mexicana SCP2-thiolase (type-2) (Lm-thiolase), complexed with acetyl-CoA and acetoacetyl-CoA, respectively, are reported. The catalytic site of thiolase contains two oxyanion holes, OAH1 and OAH2, which are important for catalysis. The two structures reveal for the first time the hydrogen bond interactions of the CoA-thioester oxygen atom of the substrate with the hydrogen bond donors of OAH1 of a CHH-thiolase. The amino acid sequence fingerprints ( xS, EAF, G P) of three catalytic loops identify the active site geometry of the well-studied CNH-thiolases, whereas SCP2-thiolases (type-1, type-2) are classified as CHH-thiolases, having as corresponding fingerprints xS, DCF and G P. In all thiolases, OAH2 is formed by the main chain NH groups of two catalytic loops. In the well-studied CNH-thiolases, OAH1 is formed by a water (of the Wat-Asn(NEAF) dyad) and NE2 (of the GHP-histidine). In the two described liganded Lm-thiolase structures, it is seen that in this CHH-thiolase, OAH1 is formed by NE2 of His338 (HDCF) and His388 (GHP). Analysis of the OAH1 hydrogen bond networks suggests that the GHP-histidine is doubly protonated and positively charged in these complexes, whereas the HDCF histidine is neutral and singly protonated.
dc.language.isoENen_US
dc.subject.enAcetyl-CoA C-Acetyltransferase
dc.subject.enCatalytic Domain
dc.subject.enCrystallography
dc.subject.enX-Ray
dc.subject.enLeishmania mexicana
dc.subject.enProtein Structure
dc.subject.enSecondary
dc.subject.enProtozoan Proteins
dc.title.enCrystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1.
dc.title.alternativeProtein Eng Des Selen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1093/protein/gzw080en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed28062645en_US
bordeaux.journalProtein Engineering, Design and Selectionen_US
bordeaux.page225-233en_US
bordeaux.volume30en_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.issue3en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcepubmed
hal.identifierhal-02348145
hal.version1
hal.date.transferred2023-11-03T16:36:00Z
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exporttrue
workflow.import.sourcepubmed
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Protein%20Engineering,%20Design%20and%20Selection&rft.date=2017-03-01&rft.volume=30&rft.issue=3&rft.spage=225-233&rft.epage=225-233&rft.eissn=1741-0134&rft.issn=1741-0134&rft.au=HARIJAN,%20Rajesh%20K&KIEMA,%20Tiila-Riikka&SYED,%20Shahan%20M&QADIR,%20Imran&MAZET,%20Muriel&rft.genre=article


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