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dc.contributor.authorLo, Chia-Hsiangen_US
dc.contributor.authorChang, Ying-Hsuanen_US
dc.contributor.authorWright, Jon D.en_US
dc.contributor.authorChen, Shih-Hsunen_US
dc.contributor.authorKan, Daphneen_US
dc.contributor.authorLim, Carmayen_US
dc.contributor.authorLiang, Po-Huangen_US
dc.date.accessioned2014-12-08T15:09:45Z-
dc.date.available2014-12-08T15:09:45Z-
dc.date.issued2009-03-25en_US
dc.identifier.issn0002-7863en_US
dc.identifier.urihttp://dx.doi.org/10.1021/ja808699cen_US
dc.identifier.urihttp://hdl.handle.net/11536/7465-
dc.description.abstractWe present here how two amino acid residues in the first helix distal from the main dimer interface modulate the dimerization and activity of a geranylgeranyl diphosphate synthase (GGPPs). The enzyme catalyzes condensation of farnesyl diphosphate and isopentenyl diphosphate to generate a C(20) product as a precursor for chlorophylls, carotenoids, and geranylgeranylated proteins. The 3D structure of GGPPs from Saccharomyces cerevisiae reveals an unique positioning of the N-terminal helix A, which protrudes into the other subunit and stabilizes dimerization, although it is far from the main dimer interface. Through a series of mutants that were characterized by analytic ultracentrifugation (AUC), the replacement of L8 and 19 at this helix with Gly was found sufficient to disrupt the dimer into a monomer, leading to at least 10(3)-fold reduction in activity. Molecular dynamics simulations and free energy decomposition analyses revealed the possible effects of the mutations on the protein structures and several critical interactions for maintaining dimerization. Further site-directed mutagenesis and AUC studies elucidated the molecular mechanism for modulating dimerization and activity by long-range interactions.en_US
dc.language.isoen_USen_US
dc.titleCombined Experimental and Theoretical Study of Long-Range Interactions Modulating Dimerization and Activity of Yeast Geranylgeranyl Diphosphate Synthaseen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/ja808699cen_US
dc.identifier.journalJOURNAL OF THE AMERICAN CHEMICAL SOCIETYen_US
dc.citation.volume131en_US
dc.citation.issue11en_US
dc.citation.spage4051en_US
dc.citation.epage4062en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.identifier.wosnumberWOS:000264792700064-
dc.citation.woscount5-
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