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Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.molcel.2020.04.014
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dc.titleCryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria
dc.contributor.authorTan, Yong Zi
dc.contributor.authorZhang, Lei
dc.contributor.authorRodrigues, Jose
dc.contributor.authorZheng, Ruixiang Blake
dc.contributor.authorGiacometti, Sabrina
dc.contributor.authorRosario, Ana L
dc.contributor.authorKloss, Brian
dc.contributor.authorDandey, Venkata P
dc.contributor.authorWei, Hui
dc.contributor.authorBrunton, Richard
dc.contributor.authorRaczkowski, Ashleigh M
dc.contributor.authorAthayde, Diogo
dc.contributor.authorCatalao, Maria Joao
dc.contributor.authorPimentel, Madalena
dc.contributor.authorClarke, Oliver B
dc.contributor.authorLowary, Todd L
dc.contributor.authorArcher, Margarida
dc.contributor.authorNiederweis, Michael
dc.contributor.authorPotter, Clinton S
dc.contributor.authorCarragher, Bridget
dc.contributor.authorMancia, Filippo
dc.date.accessioned2022-06-20T06:14:49Z
dc.date.available2022-06-20T06:14:49Z
dc.date.issued2020-05-21
dc.identifier.citationTan, Yong Zi, Zhang, Lei, Rodrigues, Jose, Zheng, Ruixiang Blake, Giacometti, Sabrina, Rosario, Ana L, Kloss, Brian, Dandey, Venkata P, Wei, Hui, Brunton, Richard, Raczkowski, Ashleigh M, Athayde, Diogo, Catalao, Maria Joao, Pimentel, Madalena, Clarke, Oliver B, Lowary, Todd L, Archer, Margarida, Niederweis, Michael, Potter, Clinton S, Carragher, Bridget, Mancia, Filippo (2020-05-21). Cryo-EM Structures and Regulation of Arabinofuranosyltransferase AftD from Mycobacteria. MOLECULAR CELL 78 (4) : 683-+. ScholarBank@NUS Repository. https://doi.org/10.1016/j.molcel.2020.04.014
dc.identifier.issn10972765
dc.identifier.issn10974164
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/227202
dc.description.abstractTan et al. present the cryo-EM structures of essential wild-type and mutant mycobacterial arabinofuranosyltransferase D (AftD), revealing the putative active site geometry and carbohydrate-binding modules. Acyl carrier protein (ACP) was tightly associated with AftD. Impairing ACP binding blocks AftD's active site, suggesting that ACP regulates enzyme function.
dc.language.isoen
dc.publisherCELL PRESS
dc.sourceElements
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectBiochemistry & Molecular Biology
dc.subjectCell Biology
dc.subjectACYL CARRIER PROTEIN
dc.subjectWALL ARABINAN BIOSYNTHESIS
dc.subjectTUBERCULOSIS CELL-WALL
dc.subjectPHOSPHATIDYLINOSITOL MANNOSIDE
dc.subjectN-GLYCOSYLATION
dc.subjectMOLECULAR-BASIS
dc.subjectIDENTIFICATION
dc.subjectARABINOGALACTAN
dc.subjectMEMBRANE
dc.subjectMODEL
dc.typeArticle
dc.date.updated2022-06-18T14:53:23Z
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1016/j.molcel.2020.04.014
dc.description.sourcetitleMOLECULAR CELL
dc.description.volume78
dc.description.issue4
dc.description.page683-+
dc.published.statePublished
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