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.articleNumber34702
dc.citation.issueNumber3
dc.citation.journalTitleStructural Dynamics
dc.citation.volumeNumber3
dc.contributor.authorCao, Hongnan
dc.contributor.authorTan, Kemin
dc.contributor.authorWang, Fengbin
dc.contributor.authorBigelow, Lance
dc.contributor.authorYennamalli, Ragothaman M.
dc.contributor.authorJedrzejczak, Robert
dc.contributor.authorBabnigg, Gyorgy
dc.contributor.authorBingman, Craig A.
dc.contributor.authorJoachimiak, Andrzej
dc.contributor.authorKharel, Madan K.
dc.contributor.authorSingh, Shanteri
dc.contributor.authorThorson, Jon S.
dc.contributor.authorPhillips, George N.Jr.
dc.date.accessioned2017-05-02T21:09:55Z
dc.date.available2017-05-02T21:09:55Z
dc.date.issued2016
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.
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.
dc.identifier.doihttp://dx.doi.org/10.1063/1.4948539
dc.identifier.urihttps://hdl.handle.net/1911/94117
dc.language.isoeng
dc.publisherAIP Publishing LLC
dc.rightsAll article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) license
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleStructural dynamics of a methionine γ-lyase for calicheamicin biosynthesis: Rotation of the conserved tyrosine stacking with pyridoxal phosphate
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpublisher version
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