The critical role of partially exposed N-terminal valine residue in stabilizing GH10 xylanase from Bacillus sp.NG-27 under poly-extreme conditions.

PloS One
Amit BhardwajVanga Siva Reddy

Abstract

Understanding the mechanisms that govern protein stability under poly-extreme conditions continues to be a major challenge. Xylanase (BSX) from Bacillus sp. NG-27, which has a TIM-barrel structure, shows optimum activity at high temperature and alkaline pH, and is resistant to denaturation by SDS and degradation by proteinase K. A comparative circular dichroism analysis was performed on native BSX and a recombinant BSX (R-BSX) with just one additional methionine resulting from the start codon. The results of this analysis revealed the role of the partially exposed N-terminus in the unfolding of BSX in response to an increase in temperature. We investigated the poly-extremophilicity of BSX to deduce the structural features responsible for its stability under one set of conditions, in order to gain information about its stability in other extreme conditions. To systematically address the role of the partially exposed N-terminus in BSX stability, a series of mutants was generated in which the first hydrophobic residue, valine (Val1), was either deleted or substituted with various amino acids. Each mutant was subsequently analyzed for its thermal, SDS and proteinase K stability in comparison to native BSX. A single conversion of Va...Continue Reading

References

Jun 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·D Goldenberg, J King
Aug 1, 1995·Current Opinion in Biotechnology·R J Russell, G L Taylor
Mar 15, 1994·European Journal of Biochemistry·B Van den BurgV G Eijsink
Jan 1, 1993·Annual Review of Biochemistry·B W Matthews
Aug 1, 1997·Current Opinion in Biotechnology·B Lee, G Vasmatzis
May 10, 2000·Nature Structural Biology·D PerlF X Schmid
Dec 12, 2001·Protein Engineering·Y MarkertR Ulbrich-Hofmann
Jul 2, 2003·Current Opinion in Microbiology·Dalia Shallom, Yuval Shoham
Jun 9, 2004·Biochemical and Biophysical Research Communications·Pochih ChangMin-Jen Tseng
Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·K ManikandanS Ramakumar
Jun 10, 2006·Journal of Molecular Biology·Hefang XieClaire Dumon

❮ Previous
Next ❯

Citations

Jan 13, 2016·World Journal of Microbiology & Biotechnology·Vishal KumarPratyoosh Shukla
Jun 22, 2017·International Journal of Biological Macromolecules·Yury A DenisenkoArkady P Sinitsyn
Jul 14, 2018·Bioscience, Biotechnology, and Biochemistry·Kota NakataniKiyoshi Yasukawa
Dec 20, 2018·Journal of Molecular Evolution·A Carl Whittington, Darin R Rokyta
Jun 3, 2021·Bioscience, Biotechnology, and Biochemistry·Kohei KuwataKiyoshi Yasukawa

❮ Previous
Next ❯

Datasets Mentioned

BETA
AF015445

Methods Mentioned

BETA
circular dichroism
gel filtration

Software Mentioned

SwissPdb Viewer
SwissPdb

Related Concepts

Related Feeds

Bacterial Protein Structures

Bacterial protein structures can expedite the development of novel antibiotics. Here is the latest research on bacterial proteins and the resolution of their structures.

Bacterial Cell Wall Structure (ASM)

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

Bacterial Cell Wall Structure

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.