Jump to main content
Jump to site search

Issue 7, 2017
Previous Article Next Article

Crystal structure of Aquifex aeolicus gene product Aq1627: a putative phosphoglucosamine mutase reveals a unique C-terminal end-to-end disulfide linkage

Author affiliations

Abstract

The Aq1627 gene from Aquifex aeolicus, a hyperthermophilic bacterium has been cloned and overexpressed in Escherichia coli. The protein was purified to homogeneity and its X-ray crystal structure was determined to 1.3 Å resolution using multiple wavelength anomalous dispersion phasing. The structural and sequence analysis of Aq1627 is suggestive of a putative phosphoglucosamine mutase. The structural features of Aq1627 further indicate that it could belong to a new subclass of the phosphoglucosamine mutase family. Aq1627 structure contains a unique C-terminal end-to-end disulfide bond, which links two monomers and this structural information can be used in protein engineering to make proteins more stable in different applications.

Graphical abstract: Crystal structure of Aquifex aeolicus gene product Aq1627: a putative phosphoglucosamine mutase reveals a unique C-terminal end-to-end disulfide linkage

Back to tab navigation

Publication details

The article was received on 24 Mar 2017, accepted on 10 May 2017 and first published on 10 May 2017


Article type: Paper
DOI: 10.1039/C7MB00182G
Citation: Mol. BioSyst., 2017,13, 1370-1376
  •   Request permissions

    Crystal structure of Aquifex aeolicus gene product Aq1627: a putative phosphoglucosamine mutase reveals a unique C-terminal end-to-end disulfide linkage

    U. Sridharan, S. Kuramitsu, S. Yokoyama, T. Kumarevel and K. Ponnuraj, Mol. BioSyst., 2017, 13, 1370
    DOI: 10.1039/C7MB00182G

Search articles by author

Spotlight

Advertisements