1P6O: The Crystal Structure Of Yeast Cytosine Deaminase Bound To 4(R)-Hydroxyl-3,4-Dihydropyrimidine At 1.14 Angstroms

Citation:
Abstract
Cytosine deaminase (CD) catalyzes the deamination of cytosine and is only present in prokaryotes and fungi, where it is a member of the pyrimidine salvage pathway. The enzyme is of interest both for antimicrobial drug design and gene therapy applications against tumors. The structure of Saccharomyces cerevisiae CD has been determined in the presence and absence of a mechanism-based inhibitor, at 1.14 and 1.43 A resolution, respectively. The enzyme forms an alpha/beta fold similar to bacterial cytidine deaminase, but with no similarity to the alpha/beta barrel fold used by bacterial cytosine deaminase or mammalian adenosine deaminase. The structures observed for bacterial, fungal, and mammalian nucleic acid deaminases represent an example of the parallel evolution of two unique protein folds to carry out the same reaction on a diverse array of substrates.
PDB ID: 1P6ODownload
MMDB ID: 24103
PDB Deposition Date: 2003/4/29
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.14  Å
Source Organism:
Similar Structures:
Biological Unit for 1P6O: dimeric; determined by author and by software (PISA)
Molecular Components in 1P6O
Label Count Molecule
Proteins (2 molecules)
2
Cytosine Deaminase(Gene symbol: FCY1)
Molecule annotation
Chemicals (9 molecules)
1
2
2
2
3
3
4
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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