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

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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

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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, Advance Article
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    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, Advance Article , DOI: 10.1039/C7MB00182G

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