Structural highlights
Publication Abstract from PubMed
The structure of thymidylate kinase from Candida albicans, determined by X-ray crystallography, is reported to a resolution of 2.45 A with a final Rfree of 0.223. Thymidylate kinase from C. albicans possesses a unique 15 residue loop that is not seen in thymidylate kinases from other genera. The structure reported here reveals that the conformation of this loop is constrained by both intra- and inter-subunit hydrogen bonding and a number of key residues in this loop are conserved among different Candida species of medical importance. The substrate specificity of the enzyme was determined using a novel NMR based assay as well as a traditional coupled assay. The enzyme is active against 3'-azido-3'-deoxythymidine (AZT) and moderately active with dGMP. The distinct functional and structural differences between the C. albicans enzyme and the human enzyme suggest that thymidylate kinase is an appropriate target for the development of new anti-fungal agents.
Structure of Thymidylate Kinase from Candida albicans Reveals a Unique Structural Element.,Sinha K, Rule GS Biochemistry. 2017 Jul 25. doi: 10.1021/acs.biochem.7b00498. PMID:28742342[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sinha K, Rule GS. Structure of Thymidylate Kinase from Candida albicans Reveals a Unique Structural Element. Biochemistry. 2017 Jul 25. doi: 10.1021/acs.biochem.7b00498. PMID:28742342 doi:http://dx.doi.org/10.1021/acs.biochem.7b00498
