Crystal structure of Aquifex aeolicus gene product Aq1627: a putative phosphoglucosamine mutase reveals a unique C-terminal end-to-end disulfide linkage. Issue 7 (26th May 2017)

• Record Type: Journal Article
• Authors: Sridharan, Upasana; Kuramitsu, Seiki; Yokoyama, Shigeyuki; Kumarevel, Thirumananseri; Ponnuraj, Karthe
• Is Part Of: Molecular bioSystems. Volume 13:Issue 7(2017)
• Page Start: 1370
• Page End: 1376
• Publication Date: 2017-05-26
• Subjects: Molecular biology -- Periodicals; Biochemistry -- Periodicals; 571.7405
• DOI: 10.1039/c7mb00182g
• Languages: English
• ISSNs: 1742-206X

Abstract

Abstract : The crystal structure of Aq 1627 protein from Aquifex aeolicus, a hyperthermophilic bacterium has been solved, which reveals a unique end-to-end disulfide linkage. Abstract : The Aq 1627 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 Aq 1627 is suggestive of a putative phosphoglucosamine mutase. The structural features of Aq 1627 further indicate that it could belong to a new subclass of the phosphoglucosamine mutase family. Aq 1627 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.