4lsi: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4lsi|  PDB=4lsi  |  SCENE=  }}
===Ion selectivity of OmpF porin soaked in 0.3M KBr===
{{ABSTRACT_PUBMED_24106986}}


The entry 4lsi is ON HOLD until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/OMPF_ECOLI OMPF_ECOLI]] Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.<ref>PMID:19721064</ref>  


Authors: Balasundaresan, D., Blachowicz, L., Roux, B.
==About this Structure==
[[4lsi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LSI OCA].  


Description: Ion selectivity of OmpF porin soaked in 0.3M KBr
==Reference==
<ref group="xtra">PMID:024106986</ref><references group="xtra"/><references/>
[[Category: Escherichia coli k-12]]
[[Category: Balasundaresan, D.]]
[[Category: Blachowicz, L.]]
[[Category: Roux, B.]]
[[Category: Beta-barrel]]
[[Category: Ion transport]]
[[Category: Outer membrane protein]]
[[Category: Porin]]
[[Category: Transport protein]]

Revision as of 06:42, 23 October 2013

Template:STRUCTURE 4lsi

Ion selectivity of OmpF porin soaked in 0.3M KBr

Template:ABSTRACT PUBMED 24106986

Function

[OMPF_ECOLI] Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.[1]

About this Structure

4lsi is a 3 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.

Reference

  1. Dhakshnamoorthy B, Ziervogel BK, Blachowicz L, Roux B. A structural study of ion permeation in OmpF porin from anomalous X-ray diffraction and molecular dynamics simulations. J Am Chem Soc. 2013 Oct 9. PMID:24106986 doi:https://dx.doi.org/10.1021/ja407783a
  1. ↑ Duval V, Nicoloff H, Levy SB. Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli. Antimicrob Agents Chemother. 2009 Nov;53(11):4944-8. doi: 10.1128/AAC.00787-09., Epub 2009 Aug 31. PMID:19721064 doi:10.1128/AAC.00787-09

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