Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii

Ashok K Rout; R Minda; D Peri; V Ramakrishnan; S K Bhattacharjee; B J Rao; K V R Chary

doi:10.1007/s12104-010-9239-4

Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii

Ashok K Rout, R Minda, D Peri, V Ramakrishnan, S K Bhattacharjee, B J Rao, K V R Chary

Institute of Chemistry and Metabolomics

8 Citations (Scopus)

Abstract

The cDNA of UVI31+ was cloned from C. reinhardtii and expressed in E. coli from where the protein was purified to homogeneity. The purified protein exhibited beta-lactamase activity (Manuscript in preparation). However, UVI31+ has no homology with the known β-lactamases. In order to understand the structural basis of the ability of UVI31+ to hydrolyze β-lactam antibiotics, we in parallel, set out to structurally characterize it by NMR. Its β-lactamase activity in relation to the solution structure by NMR is likely to provoke deeper understanding of its mechanism and facilitate the rationalization of other functions of the protein, if any. In this endeavor, we report almost complete sequence-specific backbone (1)H, (13)C and (15)N NMR assignments of UVI31+.

Original language	English
Journal	Biomolecular NMR Assignments
Volume	4
Issue number	2
Pages (from-to)	171-4
Number of pages	4
ISSN	1874-270X
DOIs	https://doi.org/10.1007/s12104-010-9239-4
Publication status	Published - 10.2010

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title = "Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii",

abstract = "The cDNA of UVI31+ was cloned from C. reinhardtii and expressed in E. coli from where the protein was purified to homogeneity. The purified protein exhibited beta-lactamase activity (Manuscript in preparation). However, UVI31+ has no homology with the known β-lactamases. In order to understand the structural basis of the ability of UVI31+ to hydrolyze β-lactam antibiotics, we in parallel, set out to structurally characterize it by NMR. Its β-lactamase activity in relation to the solution structure by NMR is likely to provoke deeper understanding of its mechanism and facilitate the rationalization of other functions of the protein, if any. In this endeavor, we report almost complete sequence-specific backbone (1)H, (13)C and (15)N NMR assignments of UVI31+.",

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doi = "10.1007/s12104-010-9239-4",

language = "English",

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T1 - Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii

AU - Rout, Ashok K

AU - Minda, R

AU - Peri, D

AU - Ramakrishnan, V

AU - Bhattacharjee, S K

AU - Rao, B J

AU - Chary, K V R

PY - 2010/10

Y1 - 2010/10

N2 - The cDNA of UVI31+ was cloned from C. reinhardtii and expressed in E. coli from where the protein was purified to homogeneity. The purified protein exhibited beta-lactamase activity (Manuscript in preparation). However, UVI31+ has no homology with the known β-lactamases. In order to understand the structural basis of the ability of UVI31+ to hydrolyze β-lactam antibiotics, we in parallel, set out to structurally characterize it by NMR. Its β-lactamase activity in relation to the solution structure by NMR is likely to provoke deeper understanding of its mechanism and facilitate the rationalization of other functions of the protein, if any. In this endeavor, we report almost complete sequence-specific backbone (1)H, (13)C and (15)N NMR assignments of UVI31+.

AB - The cDNA of UVI31+ was cloned from C. reinhardtii and expressed in E. coli from where the protein was purified to homogeneity. The purified protein exhibited beta-lactamase activity (Manuscript in preparation). However, UVI31+ has no homology with the known β-lactamases. In order to understand the structural basis of the ability of UVI31+ to hydrolyze β-lactam antibiotics, we in parallel, set out to structurally characterize it by NMR. Its β-lactamase activity in relation to the solution structure by NMR is likely to provoke deeper understanding of its mechanism and facilitate the rationalization of other functions of the protein, if any. In this endeavor, we report almost complete sequence-specific backbone (1)H, (13)C and (15)N NMR assignments of UVI31+.

U2 - 10.1007/s12104-010-9239-4

DO - 10.1007/s12104-010-9239-4

M3 - Journal articles

C2 - 20526700

SN - 1874-270X

VL - 4

SP - 171

EP - 174

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 2

ER -

Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii

Abstract

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