1p6o: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 4: Line 4:
|PDB= 1p6o |SIZE=350|CAPTION= <scene name='initialview01'>1p6o</scene>, resolution 1.14&Aring;
|PDB= 1p6o |SIZE=350|CAPTION= <scene name='initialview01'>1p6o</scene>, resolution 1.14&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HPY:4-HYDROXY-3,4-DIHYDRO-1H-PYRIMIDIN-2-ONE'>HPY</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HPY:4-HYDROXY-3,4-DIHYDRO-1H-PYRIMIDIN-2-ONE'>HPY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY= [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]  
|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= FCY1 OR YPR062W OR YP9499.17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= FCY1 OR YPR062W OR YP9499.17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|DOMAIN=
|RELATEDENTRY=[[1ox7|1OX7]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6o OCA], [http://www.ebi.ac.uk/pdbsum/1p6o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p6o RCSB]</span>
}}
}}


Line 26: Line 29:
[[Category: Ireton, G C.]]
[[Category: Ireton, G C.]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
[[Category: ACY]]
[[Category: CA]]
[[Category: HPY]]
[[Category: ZN]]
[[Category: cytosine deaminase]]
[[Category: cytosine deaminase]]
[[Category: dimer]]
[[Category: dimer]]
Line 35: Line 34:
[[Category: inhibitor bound]]
[[Category: inhibitor bound]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:20:38 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:55:36 2008''

Revision as of 19:55, 30 March 2008

File:1p6o.gif


Drag the structure with the mouse to rotate
1p6o, resolution 1.14Å
Ligands: ACY, CA, HPY, ZN
Gene: FCY1 OR YPR062W OR YP9499.17 (Saccharomyces cerevisiae)
Activity: Cytosine deaminase, with EC number 3.5.4.1
Related: 1OX7


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The crystal structure of yeast cytosine deaminase bound to 4(R)-hydroxyl-3,4-dihydropyrimidine at 1.14 angstroms.


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

1P6O is a Single protein structure of sequence from Saccharomyces cerevisiae. 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

Page seeded by OCA on Sun Mar 30 22:55:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA