Structure of the Full-Length Bacteriophytochrome from the Plant Pathogen Xanthomonas campestris Provides Clues to its Long-Range Signaling Mechanism
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- 作者：Lisandro Horacio Otero1 ; 2 ; Sebastiá ; n Klinke1 ; 2 ; Jimena Rinaldi1 ; Francisco Velá ; zquez-Escobar3 ; Marí ; a Andrea Mroginski3 ; Marí ; a Ferná ; ndez Ló ; pez3 ; Florencia Malamud4 ; Adriá ; n Alberto Vojnov5 ; Peter Hildebrandt3 ; Fernando Alberto Goldbaum1 ; 2 ; Herná ; n Ruy Bonomi1 ; hbonomi@leloir.org.ar" class="auth_mail" title="E-mail the corresponding author
- 关键词：BphP ; bacteriophytochrome ; BV ; biliverdin IXα ; GAF ; cGMP phosphodiesterase/adenylate cyclase/FhlA transcriptional activator ; HK ; histidine kinase ; MD ; molecular dynamics ; OM ; output modules ; PAS ; Period/ARNT/Single-minded ; Pfr ; far-red-absorbing ; PHY ; phytochrome specific ; Pr ; red-absorbing ; QM/MM ; quantum mechanics/molecular mechanics ; r.m.s.d. ; root-mean-square deviation ; RR ; resonance Raman ; SEC ; size exclusion chromatography ; SLS ; static-light scattering ; Xcc ; Xanthomonas campestris pv. camp
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：25 September 2016
- 年：2016
- 卷：428
- 期：19
- 页码：3702-3720
- 全文大小：3532 K
文摘
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Crystal structure of virulence-related full-length XccBphP bacteriophytochrome
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Head-to-head dimer model for full-length phytochromes confirmed at atomic scale
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Output module contributes to the helical dimer interface.
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Model for Pr–Pfr switch where output module repositions via helical spine movement