MOMP from Campylobacter jejuni Is a Trimer of 18-Stranded β-Barrel Monomers with a Ca2 + Ion Bound at the Constriction Zone
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- 作者：Luana G M Ferrara1 ; &dagger ; ; Gregor D Wallat1 ; &dagger ; ; Lucile Moynié ; 1 ; &dagger ; ; Naresh N Dhanasekar2 ; &dagger ; ; Soumeya Aliouane3 ; Silvia Acosta-Gutié ; rrez4 ; Jean-Marie Pagè ; s3 ; Jean-Michel Bolla3 ; Mathias Winterhalter2 ; Matteo Ceccarelli4 ; James H Naismith1 ; 5 ; naismith@st-andrews.ac.uk" class="auth_mail" title="E-mail the corresponding author ; naismith@st-and.ac.uk" class="auth_mail" title="E-mail the corresponding author
- 关键词：MOMP ; major outer membrane protein ; SeMet ; selenomethionine ; rMOMP ; high-resolution structure of MOMP purified from an E. coli overexpression system ; nMOMP ; high-resolution structure of MOMP purified from Campylobacter ; PEG ; polyethylene glycol ; RMSF ; root mean square fluctuations ; MD ; molecular dynamics ; Octyl-POE ; n-octylpolyoxyethylene ; CV ; column volume
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：6 November 2016
- 年：2016
- 卷：428
- 期：22
- 页码：4528-4543
- 全文大小：1786 K
文摘
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The crystal structure of MOMP, the general diffusion porin of Campylobacter, has been determined.
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The protein is an 18-stranded β-barrel that is different than the 16-stranded OmpC and OmpF proteins from E. coli, but like them, MOMP is trimeric.
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The protein has a central pore size and conductivity intermediate between OmpC and OmpF.
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A Ca2 + ion bound at the constriction zone influences the biophysical properties of porin.
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The trajectory of the transit of the antibiotic ciprofloxacin through the pore is dependent on the presence of a metal ion.