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

Timothy Knowles; DM McClelland; Sandya Rajesh; Ian Henderson; Michael Overduin

doi:10.1007/s12104-009-9175-3

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

Timothy Knowles
, DM McClelland
, Sandya Rajesh
, Ian Henderson
, Michael Overduin

Research output: Contribution to journal › Article

20 Citations (Scopus)

Abstract

We report the H-1, C-13 and N-15 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.

Original language	English
Pages (from-to)	203-206
Number of pages	4
Journal	Biomolecular NMR Assignments
Volume	3
Issue number	2
DOIs	https://doi.org/10.1007/s12104-009-9175-3
Publication status	Published - 1 Dec 2009

Keywords

NlpB
Omp85
Backbone resonance assignment
YaeT
Secondary structure
BamC
NMR

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10.1007/s12104-009-9175-3

Structural Basis of the Outer Membrane Protein Assembly System by NMR Spectroscopy
Overduin, M. (Principal Investigator), Henderson, I. (Co-Investigator) & Knowles, T. (Co-Investigator)
Biotechnology & Biological Sciences Research Council
1/12/09 → 30/11/13
Project: Research Councils
POTRA Domain Structure and Function by NMR Spectroscopy
Overduin, M. (Principal Investigator) & Henderson, I. (Co-Investigator)
Biotechnology & Biological Sciences Research Council
1/10/07 → 30/09/10
Project: Research Councils
Understanding Events at the Cell Surface During Autotransporter Biogenesis
Henderson, I. (Principal Investigator) & Overduin, M. (Co-Investigator)
Medical Research Council
10/09/07 → 9/04/11
Project: Research Councils

Cite this

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abstract = "We report the H-1, C-13 and N-15 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.",

keywords = "NlpB, Omp85, Backbone resonance assignment, YaeT, Secondary structure, BamC, NMR",

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doi = "10.1007/s12104-009-9175-3",

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AU - Knowles, Timothy

AU - McClelland, DM

AU - Rajesh, Sandya

AU - Henderson, Ian

AU - Overduin, Michael

PY - 2009/12/1

Y1 - 2009/12/1

N2 - We report the H-1, C-13 and N-15 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.

AB - We report the H-1, C-13 and N-15 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.

KW - NlpB

KW - Omp85

KW - Backbone resonance assignment

KW - YaeT

KW - Secondary structure

KW - BamC

KW - NMR

U2 - 10.1007/s12104-009-9175-3

DO - 10.1007/s12104-009-9175-3

M3 - Article

C2 - 19888691

VL - 3

SP - 203

EP - 206

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 2

ER -

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

Abstract

Keywords

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Projects

Structural Basis of the Outer Membrane Protein Assembly System by NMR Spectroscopy

POTRA Domain Structure and Function by NMR Spectroscopy

Understanding Events at the Cell Surface During Autotransporter Biogenesis

Cite this