1ox7
From Proteopedia
(New page: 200px<br /><applet load="1ox7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ox7, resolution 1.43Å" /> '''Crystal structure of...) |
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| - | [[Image:1ox7.gif|left|200px]]<br /><applet load="1ox7" size=" | + | [[Image:1ox7.gif|left|200px]]<br /><applet load="1ox7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ox7, resolution 1.43Å" /> | caption="1ox7, resolution 1.43Å" /> | ||
'''Crystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound'''<br /> | '''Crystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytosine deaminase (CD) catalyzes the deamination of cytosine and is only | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1OX7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytosine_deaminase Cytosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.1 3.5.4.1] Full crystallographic information is available from [http:// | + | 1OX7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytosine_deaminase Cytosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.1 3.5.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OX7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Black, M | + | [[Category: Black, M E.]] |
| - | [[Category: Ireton, G | + | [[Category: Ireton, G C.]] |
| - | [[Category: Stoddard, B | + | [[Category: Stoddard, B L.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: aminohydrolase]] | [[Category: aminohydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:41 2008'' |
Revision as of 12:22, 21 February 2008
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Crystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound
Overview
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.
About this Structure
1OX7 is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Cytosine deaminase, with EC number 3.5.4.1 Full crystallographic information is available from OCA.
Reference
The 1.14 A crystal structure of yeast cytosine deaminase: evolution of nucleotide salvage enzymes and implications for genetic chemotherapy., Ireton GC, Black ME, Stoddard BL, Structure. 2003 Aug;11(8):961-72. PMID:12906827
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