An Aromatic Cap Seals the Substrate Binding Site in an ECF-Type S Subunit for Riboflavin
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- 作者：Nathan K. Karpowich ; Nathan.Karpowich@med.nyu.edu" class="auth_mail" title="E-mail the corresponding author ; Jinmei Song ; Da-Neng Wang ; Da-Neng.Wang@med.nyu.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：ECF ; energy coupling factor ; TM ; transmembrane ; NG ; nonyl glucoside ; SEC ; size exclusion chromatography ; MALLS ; multi-angle laser light scattering ; H-bonds ; hydrogen bonds ; FMN ; flavin mononucleotide ; PLY ; Pro-Leu-Tyr ; MD ; molecular dynamics ; FSEC ; fluorescence size exclusion chromatography ; DDM ; dodecyl-maltoside ; PEG ; polyethylene glycol
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：31 July 2016
- 年：2016
- 卷：428
- 期：15
- 页码：3118-3130
- 全文大小：1639 K
文摘
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The conformational changes upon substrate binding to EcfS proteins are unknown.
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Riboflavin-bound TmRibU is exceptionally stable compared to other membrane proteins.
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Seven of eight available riboflavin H-bonds are satisfied upon binding to TmRibU.
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A conserved aromatic residue in TM5, Tyr130, caps the substrate binding site.
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This aromatic capping interaction is essential for high-affinity substrate binding.
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