¹H, ¹³C and ¹⁵N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis

Qingxin Li; Angela Shuyi Chen; Shovanlal Gayen; Congbao Kang

doi:10.1007/s12104-012-9392-z

¹H, ¹³C and ¹⁵N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis

Biomol NMR Assign. 2013 Oct;7(2):129-32. doi: 10.1007/s12104-012-9392-z. Epub 2012 May 15.

Authors

Qingxin Li¹, Angela Shuyi Chen, Shovanlal Gayen, Congbao Kang

Affiliation

¹ Institute of Chemical and Engineering Sciences, Agency for Science, Technology and Research, Singapore, Singapore.

PMID: 22585087
DOI: 10.1007/s12104-012-9392-z

Abstract

Intracellular proteinases (ISPs) are the main component of the bacilli degradome and a distinctive class in different bacilli. An intracellular proteinase inhibitor of the bacteria Bacillus subtillis was shown to regulate the activity of ISP-1. To study the structure of this inhibitor, we report the resonance assignment for this protein with 119 amino acid. The data will allow us to perform structural study on this inhibitor to understand its mechanism for ISP-1 inhibition.

Publication types

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

MeSH terms

Amino Acid Sequence
Bacillus subtilis / metabolism*
Bacterial Proteins / chemistry*
Carbon Isotopes
Intracellular Space / metabolism*
Molecular Sequence Data
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular*
Protease Inhibitors / chemistry*
Protein Structure, Secondary
Protons*

Substances

Bacterial Proteins
Carbon Isotopes
Nitrogen Isotopes
Protease Inhibitors
Protons