Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli

Timothy J Knowles; Darren M McClelland; Sandya Rajesh; Ian R Henderson; Michael Overduin

doi:10.1007/s12104-009-9175-3

Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli

Biomol NMR Assign. 2009 Dec;3(2):203-6. doi: 10.1007/s12104-009-9175-3. Epub 2009 Jun 24.

Authors

Timothy J Knowles¹, Darren M McClelland, Sandya Rajesh, Ian R Henderson, Michael Overduin

Affiliation

¹ School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. [email protected]

PMID: 19888691
DOI: 10.1007/s12104-009-9175-3

Abstract

We report the (1)H, (13)C and (15)N backbone chemical shift assignments and secondary structure of the Escherichia coli protein BamC, a 32-kDa protein subunit that forms part of the BAM (Omp85) complex, the beta-barrel assembly machinery present in all Gram-negative bacteria and which is essential for viability.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Outer Membrane Proteins / chemistry*
Bacterial Outer Membrane Proteins / metabolism
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / metabolism
Escherichia coli*
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary

Substances

Bacterial Outer Membrane Proteins
Escherichia coli Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding