1ux0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ux0.gif|left|200px]]<br /><applet load="1ux0" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ux0.gif|left|200px]]
-
caption="1ux0, resolution 1.99&Aring;" />
+
 
-
'''BACILLUS SUBTILIS CYTIDINE DEAMINASE WITH AN ARG56- GLN SUBSTITUTION'''<br />
+
{{Structure
 +
|PDB= 1ux0 |SIZE=350|CAPTION= <scene name='initialview01'>1ux0</scene>, resolution 1.99&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Thu+Binding+Site+For+Chain+B'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=THU:TETRAHYDRODEOXYURIDINE'>THU</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]
 +
|GENE=
 +
}}
 +
 
 +
'''BACILLUS SUBTILIS CYTIDINE DEAMINASE WITH AN ARG56- GLN SUBSTITUTION'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1UX0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=THU:'>THU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Thu+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UX0 OCA].
+
1UX0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UX0 OCA].
==Reference==
==Reference==
-
Structural, kinetic, and mutational studies of the zinc ion environment in tetrameric cytidine deaminase., Johansson E, Neuhard J, Willemoes M, Larsen S, Biochemistry. 2004 May 25;43(20):6020-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15147186 15147186]
+
Structural, kinetic, and mutational studies of the zinc ion environment in tetrameric cytidine deaminase., Johansson E, Neuhard J, Willemoes M, Larsen S, Biochemistry. 2004 May 25;43(20):6020-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15147186 15147186]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Cytidine deaminase]]
[[Category: Cytidine deaminase]]
Line 28: Line 37:
[[Category: zinc binding]]
[[Category: zinc binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:13 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:37:55 2008''

Revision as of 12:37, 20 March 2008

Image:1ux0.gif


PDB ID 1ux0

Drag the structure with the mouse to rotate
, resolution 1.99Å
Sites:
Ligands: and
Activity: Cytidine deaminase, with EC number 3.5.4.5
Coordinates: save as pdb, mmCIF, xml



BACILLUS SUBTILIS CYTIDINE DEAMINASE WITH AN ARG56- GLN SUBSTITUTION


Overview

The zinc-containing cytidine deaminase (CDA, EC 3.5.4.5) is a pyrimidine salvage enzyme catalyzing the hydrolytic deamination of cytidine and 2'-deoxycytidine forming uridine and 2'-deoxyuridine, respectively. Homodimeric CDA (D-CDA) and homotetrameric CDA (T-CDA) both contain one zinc ion per subunit coordinated to the catalytic water molecule. The zinc ligands in D-CDA are one histidine and two cysteine residues, whereas in T-CDA zinc is coordinated to three cysteines. Two of the zinc coordinating cysteines in T-CDA form hydrogen bonds to the conserved residue Arg56, and this residue together with the dipole moments from two alpha-helices partially neutralizes the additional negative charge in the active site, leading to a catalytic activity similar to D-CDA. Arg56 has been substituted by a glutamine (R56Q), the corresponding residue in D-CDA, an alanine (R56A), and an aspartate (R56D). Moreover, one of the zinc-liganding cysteines has been substituted by histidine to mimic D-CDA, alone (C53H) and in combination with R56Q (C53H/R56Q). R56A, R56Q, and C53H/R56Q contain the same amount of zinc as the wild-type enzyme. The zinc-binding capacity of R56D is reduced. Only R56A, R56Q, and C53H/R56Q yielded measurable CDA activity, R56A and R56Q with similar K(m) but decreased V(max) values compared to wild-type enzyme. Because of dissociation into its inactive subunits, it was impossible to determine the kinetic parameters for C53H/R56Q. R56A and C53H/R56Q display increased apparent pK(a) values compared to the wild-type enzyme and R56Q. On the basis of the structures of R56A, R56Q, and C53H/R56Q an explanation is provided of kinetic results and the apparent instability of C53H/R56Q.

About this Structure

1UX0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Structural, kinetic, and mutational studies of the zinc ion environment in tetrameric cytidine deaminase., Johansson E, Neuhard J, Willemoes M, Larsen S, Biochemistry. 2004 May 25;43(20):6020-9. PMID:15147186

Page seeded by OCA on Thu Mar 20 14:37:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ux0"
Personal tools