NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond

Robert Mark Hagan; Ragnar Bjornsson; Stephen McMahon; B Schomburg; V Braithwaite; Michael Buehl; Jim Naismith; Uli Schwarz-Linek

doi:10.1002/anie.201004340

NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond

Robert Mark Hagan, Ragnar Bjornsson, Stephen McMahon, B Schomburg, V Braithwaite, Michael Buehl, Jim Naismith, Uli Schwarz-Linek

Research output: Contribution to journal › Article › peer-review

Abstract

One bond makes all the difference: Three suitably positioned amino acid side chains (see picture) and a hydrophobic environment are all that is required for an amidation reaction with remarkable consequences. An emerging central building block of bacterial surface proteins owes its stability to a spontaneously formed isopeptide bond. The impact of this bond on protein structure and dynamics and the mechanism of its formation are scrutinized in detail.

Original language	English
Pages (from-to)	8421-8425
Number of pages	5
Journal	Angewandte Chemie International Edition
Volume	49
Issue number	45
Early online date	28 Sept 2010
DOIs	https://doi.org/10.1002/anie.201004340
Publication status	Published - Nov 2010

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10.1002/anie.201004340

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abstract = "One bond makes all the difference: Three suitably positioned amino acid side chains (see picture) and a hydrophobic environment are all that is required for an amidation reaction with remarkable consequences. An emerging central building block of bacterial surface proteins owes its stability to a spontaneously formed isopeptide bond. The impact of this bond on protein structure and dynamics and the mechanism of its formation are scrutinized in detail.",

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AU - Hagan, Robert Mark

AU - Bjornsson, Ragnar

AU - McMahon, Stephen

AU - Schomburg, B

AU - Braithwaite, V

AU - Buehl, Michael

AU - Naismith, Jim

AU - Schwarz-Linek, Uli

PY - 2010/11

Y1 - 2010/11

N2 - One bond makes all the difference: Three suitably positioned amino acid side chains (see picture) and a hydrophobic environment are all that is required for an amidation reaction with remarkable consequences. An emerging central building block of bacterial surface proteins owes its stability to a spontaneously formed isopeptide bond. The impact of this bond on protein structure and dynamics and the mechanism of its formation are scrutinized in detail.

AB - One bond makes all the difference: Three suitably positioned amino acid side chains (see picture) and a hydrophobic environment are all that is required for an amidation reaction with remarkable consequences. An emerging central building block of bacterial surface proteins owes its stability to a spontaneously formed isopeptide bond. The impact of this bond on protein structure and dynamics and the mechanism of its formation are scrutinized in detail.

UR - https://www.scopus.com/pages/publications/78149435900

UR - http://ukpmc.ac.uk/abstract/MED/20878961

U2 - 10.1002/anie.201004340

DO - 10.1002/anie.201004340

M3 - Article

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VL - 49

SP - 8421

EP - 8425

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

IS - 45

ER -

NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond

Abstract

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Carb Export: Bacteria Ref: 081862/Z/06/Z: Carbohydrate export in bacteria

BBSRC BBS/B/14426: SPORT

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NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond

Abstract

Access to Document

Other files and links

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Projects

Carb Export: Bacteria Ref: 081862/Z/06/Z: Carbohydrate export in bacteria

BBSRC BBS/B/14426: SPORT

Cite this