2WVP: Synthetically Modified Ompg

Citation:
Abstract
Chemical modification of ion channels has recently attracted attention due to their potential use in stochastic sensing and neurobiology. Among the available channel templates stable beta-barrel proteins have shown their potential for large scale chemical modifications due to their wide pore lumen. Ion-channel hybrids using the outer membrane protein OmpG were generated by S-alkylation with a synthetic modulator and functionally as well as structurally characterized. The dansyl moiety of the used modulator resulted in partial blockage of current though the OmpG channel with its gating characteristics mainly unaffected. The crystal structure of an OmpG-dansyl hybrid at 2.4A resolution correlates this finding by showing that the modulator lines the inner walling of the OmpG pore. These results underline the suitability of OmpG as a structural base for the construction of stochastic sensors.
PDB ID: 2WVPDownload
MMDB ID: 83259
PDB Deposition Date: 2009/10/19
Updated in MMDB: 2010/07
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 2WVP: monomeric; determined by author and by software (PISA)
Molecular Components in 2WVP
Label Count Molecule
Protein (1 molecule)
1
Outer Membrane Protein G(Gene symbol: ompG)
Molecule annotation
Chemicals (8 molecules)
1
1
2
6
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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