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6GWU

Carbonic anhydrase CaNce103p from Candida albicans

Summary for 6GWU
Entry DOI10.2210/pdb6gwu/pdb
DescriptorCarbonic anhydrase, ZINC ION, BETA-MERCAPTOETHANOL, ... (6 entities in total)
Functional Keywordscarbonic anhydrase, candida albicans, cance103p, substrate tunnel, lyase
Biological sourceCandida albicans (Yeast)
Total number of polymer chains4
Total formula weight93197.89
Authors
Brynda, J.,Dostal, J.,Heidingsfeld, O.,Machacek, S.,Blaha, J.,Pichova, I. (deposition date: 2018-06-26, release date: 2018-11-07, Last modification date: 2024-01-17)
Primary citationDostal, J.,Brynda, J.,Blaha, J.,Machacek, S.,Heidingsfeld, O.,Pichova, I.
Crystal structure of carbonic anhydrase CaNce103p from the pathogenic yeast Candida albicans.
BMC Struct. Biol., 18:14-14, 2018
Cited by
PubMed Abstract: The pathogenic yeast Candida albicans can proliferate in environments with different carbon dioxide concentrations thanks to the carbonic anhydrase CaNce103p, which accelerates spontaneous conversion of carbon dioxide to bicarbonate and vice versa. Without functional CaNce103p, C. albicans cannot survive in atmospheric air. CaNce103p falls into the β-carbonic anhydrase class, along with its ortholog ScNce103p from Saccharomyces cerevisiae. The crystal structure of CaNce103p is of interest because this enzyme is a potential target for surface disinfectants.
PubMed: 30367660
DOI: 10.1186/s12900-018-0093-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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