Structural dynamics of a methionine γ-lyase for calicheamicin biosynthesis: Rotation of the conserved tyrosine stacking with pyridoxal phosphate

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dc.citation.articleNumber34702en_US
dc.citation.issueNumber3en_US
dc.citation.journalTitleStructural Dynamicsen_US
dc.citation.volumeNumber3en_US
dc.contributor.authorCao, Hongnanen_US
dc.contributor.authorTan, Keminen_US
dc.contributor.authorWang, Fengbinen_US
dc.contributor.authorBigelow, Lanceen_US
dc.contributor.authorYennamalli, Ragothaman M.en_US
dc.contributor.authorJedrzejczak, Roberten_US
dc.contributor.authorBabnigg, Gyorgyen_US
dc.contributor.authorBingman, Craig A.en_US
dc.contributor.authorJoachimiak, Andrzejen_US
dc.contributor.authorKharel, Madan K.en_US
dc.contributor.authorSingh, Shanterien_US
dc.contributor.authorThorson, Jon S.en_US
dc.contributor.authorPhillips, George N.Jr.en_US
dc.date.accessioned2017-05-02T21:09:55Zen_US
dc.date.available2017-05-02T21:09:55Zen_US
dc.date.issued2016en_US
dc.description.abstractCalE6 from Micromonospora echinospora is a (pyridoxal 5′ phosphate) PLP-dependent methionine γ-lyase involved in the biosynthesis of calicheamicins. We report the crystal structure of a CalE6 2-(N-morpholino)ethanesulfonic acid complex showing ligand-induced rotation of Tyr100, which stacks with PLP, resembling the corresponding tyrosine rotation of true catalytic intermediates of CalE6 homologs. Elastic network modeling and crystallographic ensemble refinement reveal mobility of the N-terminal loop, which involves both tetrameric assembly and PLP binding. Modeling and comparative structural analysis of PLP-dependent enzymes involved in Cys/Met metabolism shine light on the functional implications of the intrinsic dynamic properties of CalE6 in catalysis and holoenzyme maturation.en_US
dc.identifier.citationCao, Hongnan, Tan, Kemin, Wang, Fengbin, et al.. "Structural dynamics of a methionine γ-lyase for calicheamicin biosynthesis: Rotation of the conserved tyrosine stacking with pyridoxal phosphate." <i>Structural Dynamics,</i> 3, no. 3 (2016) AIP Publishing LLC: http://dx.doi.org/10.1063/1.4948539.en_US
dc.identifier.doihttp://dx.doi.org/10.1063/1.4948539en_US
dc.identifier.urihttps://hdl.handle.net/1911/94117en_US
dc.language.isoengen_US
dc.publisherAIP Publishing LLCen_US
dc.rightsAll article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) licenseen_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en_US
dc.titleStructural dynamics of a methionine γ-lyase for calicheamicin biosynthesis: Rotation of the conserved tyrosine stacking with pyridoxal phosphateen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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