1ox7: Difference between revisions

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[[Image:1ox7.~~gif~~|left|200px]]

[[Image:1ox7.png|left|200px]]

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~~'''~~Crystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound~~'''~~

===Crystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12906827}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12906827 is the PubMed ID number.

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==About this Structure==

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[[Category: Stoddard, B L.]]

[[Category: Aminohydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 04~~:23:24 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:57:51 2008''

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-[[Image:1ox7.gif|left|200px]]
+{{Seed}}
+[[Image:1ox7.png|left|200px]]
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 {{STRUCTURE_1ox7|  PDB=1ox7  |  SCENE=  }}
-'''Crystal structure of yeast cytosine deaminase apo-enzyme: inorganic zinc bound'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12906827}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12906827 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12906827}}
 ==About this Structure==
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 [[Category: Stoddard, B L.]]
 [[Category: Aminohydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:23:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:57:51 2008''