Abstract
The bacterial immunoglobulin-like (Big) domain is one of the prevalent domain types, which facilitates cell–cell adhesion by assembling into multi-domain architectures. We selected a four Big_2 domain protein (named ‘Arig’) from a Gram positive, Paenarthrobacter aurescens TC1 (known earlier as Arthrobacter aurescens TC1). In an attempt to characterize structural and ligand-binding features of individual Big_2 domains, we have cloned, overexpressed, isolated and purified the second Big_2 domain of Arig along with a few of its adjacent Big_2 domain residues (residue 143 to 269) referred to as ‘Arig2’. The 13C/15N-doubly-labeled His-tagged Arig2 (133 residues long) showed an ordered conformation as revealed by the well dispersed 2D [15N-1H]-HSQC spectrum. Subsequently, a suite of heteronuclear 3D NMR experiments has enabled almost complete 1H, 13C and 15N NMR resonance assignments of Arig2.
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Abbreviations
- Arig2:
-
Second Big_2 domain of Arig protein
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Acknowledgements
The facilities provided by the National Facility for High Field NMR, supported by the Department of Science and Technology (DST), Department of Biotechnology (DBT), Council of Scientific and Industrial Research (CSIR), and Tata Institute of Fundamental Research (TIFR), Mumbai, are gratefully acknowledged. We acknowledge the financial support of CSIR (BSC0120) to YS and JC Bose Fellowship of DST (Govt. of India) to KVRC. AP is supported by a Senior Research fellowship of UGC, India. DV acknowledges the research fellowship of Tata Institute of Fundamental Research, Government of India.
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AP and VD have contributed equally to the work.
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Pawar, A.D., Verma, D., Raman, R. et al. 1H, 13C and 15N NMR assignments of a bacterial immunoglobulin-like domain (group 2) of a protein of a bacterium Paenarthrobacter aurescens TC1. Biomol NMR Assign 11, 203–206 (2017). https://doi.org/10.1007/s12104-017-9748-5
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DOI: https://doi.org/10.1007/s12104-017-9748-5