1jtk: Difference between revisions

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|PDB= 1jtk |SIZE=350|CAPTION= <scene name='initialview01'>1jtk</scene>, resolution 2.04&Aring;
|PDB= 1jtk |SIZE=350|CAPTION= <scene name='initialview01'>1jtk</scene>, resolution 2.04&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=THU:TETRAHYDRODEOXYURIDINE'>THU</scene>
|LIGAND= <scene name='pdbligand=THU:TETRAHYDRODEOXYURIDINE'>THU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Cytidine_deaminase Cytidine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.5 3.5.4.5]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytidine_deaminase Cytidine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.5 3.5.4.5] </span>
|GENE= cdd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
|GENE= cdd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jtk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jtk OCA], [http://www.ebi.ac.uk/pdbsum/1jtk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jtk RCSB]</span>
}}
}}


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[[Category: Mejlhede, N.]]
[[Category: Mejlhede, N.]]
[[Category: Neuhard, J.]]
[[Category: Neuhard, J.]]
[[Category: THU]]
[[Category: ZN]]
[[Category: cda]]
[[Category: cda]]
[[Category: cytidine deaminase]]
[[Category: cytidine deaminase]]
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[[Category: zinc]]
[[Category: zinc]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:08:17 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:50 2008''

Revision as of 21:38, 30 March 2008

File:1jtk.gif


PDB ID 1jtk

Drag the structure with the mouse to rotate
, resolution 2.04Å
Ligands: ,
Gene: cdd (Bacillus subtilis)
Activity: Cytidine deaminase, with EC number 3.5.4.5
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of cytidine deaminase from Bacillus subtilis in complex with the inhibitor tetrahydrodeoxyuridine


OverviewOverview

Cytidine deaminases (CDA, EC 3.5.4.5) are zinc-containing enzymes in the pyrimidine salvage pathway that catalyze the formation of uridine and deoxyuridine from cytidine and deoxycytidine, respectively. Two different classes have been identified in the CDA family, a homodimeric form (D-CDA) with two zinc ions per dimer and a homotetrameric form (T-CDA) with four zinc ions per tetramer. We have determined the first structure of a T-CDA from Bacillus subtilis. The active form of T-CDA is assembled of four identical subunits with one active site apiece. The subunit of D-CDA is composed of two domains each exhibiting the same fold as the T-CDA subunits, but only one of them contains zinc in the active site. The similarity results in a conserved structural core in the two CDA forms. An intriguing difference between the two CDA structures is the zinc coordinating residues found at the N-terminal of two alpha-helices: three cysteine residues in the tetrameric form and two cysteine residues and one histidine residue in the dimeric form. The role of the zinc ion is to activate a water molecule and thereby generate a hydroxide ion. How the zinc ion in T-CDA surrounded with three negatively charged residues can create a similar activity of T-CDA compared to D-CDA has been an enigma. However, the structure of T-CDA reveals that the negative charge caused by the three ligands is partly neutralized by (1) an arginine residue hydrogen-bonded to two of the cysteine residues and (2) the dipoles of two alpha-helices.

About this StructureAbout this Structure

1JTK is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 A resolution., Johansson E, Mejlhede N, Neuhard J, Larsen S, Biochemistry. 2002 Feb 26;41(8):2563-70. PMID:11851403

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