2WVP

Synthetically modified OmpG

Summary for 2WVP

• Entry DOI: 10.2210/pdb2wvp/pdb
• Related: 2F1C 2IWV 2IWW
• Descriptor: OUTER MEMBRANE PROTEIN G, N-[2-({[5-(DIMETHYLAMINO)NAPHTHALEN-1-YL]SULFONYL}AMINO)ETHYL]-2-IODOACETAMIDE, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (5 entities in total)
• Functional Keywords: ion-channel engineering, ompg hybrids, membrane protein
• Biological source: ESCHERICHIA COLI
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P76045
• Total number of polymer chains: 1
• Total formula weight: 35936.19

Authors

Grosse, W.,Reiss, P.,Reitz, S.,Cebi, M.,Luebben, W.,Koert, U.,Essen, L.-O. (deposition date: 2009-10-19, release date: 2010-07-14, Last modification date: 2024-11-13)

Primary citation

Grosse, W.,Reiss, P.,Reitz, S.,Cebi, M.,Luebben, W.,Koert, U.,Essen, L.-O.
Structural and Functional Characterization of a Synthetically Modified Ompg.
Bioorg.Med.Chem., 18:7716-, 2010

PubMed 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 β-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 2.4Å 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.

PubMed: 20378361
DOI: 10.1016/J.BMC.2010.03.044

Experimental method

X-RAY DIFFRACTION (2.4 Å)