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  Role of N-terminal region of Escherichia coli maltodextrin glucosidase in folding and function of the protein

Pastor, A., Singh, A. K., Shukla, P. K., Equbal, M. J., Malik, S. T., Singh, T. P., et al. (2016). Role of N-terminal region of Escherichia coli maltodextrin glucosidase in folding and function of the protein. Biochimica et Biophysica Acta-Proteins and Proteomics, 1864(9), 1138-1151. doi:10.1016/j.bbapap.2016.06.008.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-53DE-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-53DF-E
Genre: Journal Article

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 Creators:
Pastor, Ashutosh1, Author
Singh, Amit K.2, Author              
Shukla, Prakash K.1, Author
Equbal, Md. Javed1, Author
Malik, Shikha T.1, Author
Singh, Tej P.1, Author
Chaudhuri, Tapan K.1, Author
Affiliations:
1external, ou_persistent22              
2Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

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Free keywords: VULGARIS R-47 ALPHA-AMYLASE-1; ALPHA-AMYLASES; CHAPERONIN GROEL; LIMITED PROTEOLYSIS; CIRCULAR-DICHROISM; DISORDERED REGIONS; PREDICTION; SYSTEM; DOMAIN; POLYPEPTIDEBiochemistry & Molecular Biology; Biophysics; Protein folding; GroEL assisted protein folding; Protein structure and function; Maltodextrin glucosidase; X-ray crystallography;
 Abstract: Maltodextrin glucosidase (MalZ) hydrolyses short malto-oligosaccharides from the reducing end releasing glucose and maltose in Escherichia coli. MalZ is a highly aggregation prone protein and molecular chaperonins GroEL and GroES assist in the folding of this protein to a substantial level. The N-terminal region of this enzyme appears to be a unique domain as seen in sequence comparison studies with other amylases as well as through homology modelling. The sequence and homology model analysis show a probability of disorder in the N-Terminal region of MaIZ. The crystal structure of this enzyme has been reported in the present communication. Based on the crystallographic structure, it has been interpreted that the N-terminal region of the enzyme (Met1-Phe131) might be unstructured or flexible. To understand the role of the N-terminal region of MaIZ in its enzymatic activity, and overall stability, a truncated version (Ala111-His616) of MaIZ was created. The truncated version failed to fold into an active enzyme both in E. coli cytosol and in vitro even with the assistance of chaperonins GroEL and GroES. Furthermore, the refolding effort of N-truncated MaIZ in the presence of isolated N-terminal domain didn't succeed. Our studies suggest that while the structural rigidity or orientation of the N-terminal region of the MalZ protein may not be essential for its stability and function, but the said domain is likely to play an important role in the formation of the native structure of the protein when present as an integral part of the protein. (C) 2016 Elsevier B.V. All rights reserved.

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Language(s): eng - English
 Dates: 2016-01-142016-06-142016-06-162016
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
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Title: Biochimica et Biophysica Acta-Proteins and Proteomics
  Other : BBA-Proteins Proteomics
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1864 (9) Sequence Number: - Start / End Page: 1138 - 1151 Identifier: ISSN: 1570-9639
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_5