Abstract
AbstractKlebsiella pneumoniae (KP), a Gram‐negative bacterium, is a common cause of hospital‐acquired bacterial infections worldwide. Tellurium (Te) compounds, although relatively rare in the environment, have a long history as antimicrobial and therapeutic agents. In bacteria, tellurite (TeO3 −2) resistance is conferred by the ter (Ter) operon (terZABCDEF). Here, on the basis of 2593 restraints derived from NMR analysis, we report the NMR structure of TerB protein (151 amino acids) of KP (KP‐TerB), which is mainly composed of seven α‐helices and a 310 helix, with helices II to V apparently forming a four‐helix bundle. The ensemble of 20 NMR structures was well‐defined, with a RMSD of 0.32 ± 0.06 Å for backbone atoms and 1.11 ± 0.07 Å for heavy atoms, respectively. A unique property of the KP‐TerB structure is that the positively and negatively charged clusters are formed by the N‐terminal positively and C‐terminal negatively charged residues, respectively. To the best of our knowledge, the protein sequence and structures of KP‐TerB are unique.
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Dates
Type | When |
---|---|
Created | 17 years, 6 months ago (Feb. 27, 2008, 9:39 p.m.) |
Deposited | 1 year, 11 months ago (Sept. 29, 2023, 12:52 a.m.) |
Indexed | 1 year, 1 month ago (July 23, 2024, 10:21 p.m.) |
Issued | 17 years, 5 months ago (April 1, 2008) |
Published | 17 years, 5 months ago (April 1, 2008) |
Published Online | 16 years, 8 months ago (Jan. 2, 2009) |
Published Print | 17 years, 5 months ago (April 1, 2008) |
@article{Chiang_2008, title={NMR solution structure of KP‐TerB, a tellurite‐resistance protein from Klebsiella pneumoniae}, volume={17}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.073389408}, DOI={10.1110/ps.073389408}, number={4}, journal={Protein Science}, publisher={Wiley}, author={Chiang, Sheng‐Kuo and Lou, Yuan‐Chao and Chen, Chinpan}, year={2008}, month=apr, pages={785–789} }