Show simple item record

dc.contributor.authorCao, Hongnan
Tan, Kemin
Wang, Fengbin
Bigelow, Lance
Yennamalli, Ragothaman M.
Jedrzejczak, Robert
Babnigg, Gyorgy
Bingman, Craig A.
Joachimiak, Andrzej
Kharel, Madan K.
Singh, Shanteri
Thorson, Jon S.
Phillips, George N. Jr.
dc.date.accessioned 2017-05-02T21:09:55Z
dc.date.available 2017-05-02T21:09:55Z
dc.date.issued 2016
dc.identifier.citation Cao, 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." Structural Dynamics, 3, no. 3 (2016) AIP Publishing LLC: http://dx.doi.org/10.1063/1.4948539.
dc.identifier.urihttps://hdl.handle.net/1911/94117
dc.description.abstract CalE6 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.language.iso eng
dc.publisher AIP Publishing LLC
dc.rights All 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.title Structural dynamics of a methionine γ-lyase for calicheamicin biosynthesis: Rotation of the conserved tyrosine stacking with pyridoxal phosphate
dc.type Journal article
dc.citation.journalTitle Structural Dynamics
dc.citation.volumeNumber 3
dc.citation.issueNumber 3
dc.type.dcmi Text
dc.identifier.doihttp://dx.doi.org/10.1063/1.4948539
dc.identifier.pmcid PMC4851618
dc.identifier.pmid 27191010
dc.type.publication publisher version
dc.citation.articleNumber 034702


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record