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1uw8

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[[Image:1uw8.gif|left|200px]]<br /><applet load="1uw8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1uw8.gif|left|200px]]
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caption="1uw8, resolution 2.00&Aring;" />
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'''CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE'''<br />
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{{Structure
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|PDB= 1uw8 |SIZE=350|CAPTION= <scene name='initialview01'>1uw8</scene>, resolution 2.00&Aring;
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|SITE= <scene name='pdbsite=AC1:Trs+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Oxalate_decarboxylase Oxalate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.2 4.1.1.2]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UW8 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=MN:'>MN</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Oxalate_decarboxylase Oxalate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.2 4.1.1.2] Known structural/functional Site: <scene name='pdbsite=AC1:Trs+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UW8 OCA].
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1UW8 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=1UW8 OCA].
==Reference==
==Reference==
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A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site., Just VJ, Stevenson CE, Bowater L, Tanner A, Lawson DM, Bornemann S, J Biol Chem. 2004 May 7;279(19):19867-74. Epub 2004 Feb 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14871895 14871895]
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A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site., Just VJ, Stevenson CE, Bowater L, Tanner A, Lawson DM, Bornemann S, J Biol Chem. 2004 May 7;279(19):19867-74. Epub 2004 Feb 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14871895 14871895]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Oxalate decarboxylase]]
[[Category: Oxalate decarboxylase]]
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[[Category: oxalate]]
[[Category: oxalate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:37:37 2008''

Revision as of 12:37, 20 March 2008

Image:1uw8.gif


PDB ID 1uw8

Drag the structure with the mouse to rotate
, resolution 2.00Å
Sites:
Ligands: and
Activity: Oxalate decarboxylase, with EC number 4.1.1.2
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE


Overview

Oxalate decarboxylase (EC 4.1.1.2) catalyzes the conversion of oxalate to formate and carbon dioxide and utilizes dioxygen as a cofactor. By contrast, the evolutionarily related oxalate oxidase (EC 1.2.3.4) converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. Divergent free radical catalytic mechanisms have been proposed for these enzymes that involve the requirement of an active site proton donor in the decarboxylase but not the oxidase reaction. The oxidase possesses only one domain and manganese binding site per subunit, while the decarboxylase has two domains and two manganese sites per subunit. A structure of the decarboxylase together with a limited mutagenesis study has recently been interpreted as evidence that the C-terminal domain manganese binding site (site 2) is the catalytic site and that Glu-333 is the crucial proton donor (Anand, R., Dorrestein, P. C., Kinsland, C., Begley, T. P., and Ealick, S. E. (2002) Biochemistry 41, 7659-7669). The N-terminal binding site (site 1) of this structure is solvent-exposed (open) and lacks a suitable proton donor for the decarboxylase reaction. We report a new structure of the decarboxylase that shows a loop containing a 3(10) helix near site 1 in an alternative conformation. This loop adopts a "closed" conformation forming a lid covering the entrance to site 1. This conformational change brings Glu-162 close to the manganese ion, making it a new candidate for the crucial proton donor. Site-directed mutagenesis of equivalent residues in each domain provides evidence that Glu-162 performs this vital role and that the N-terminal domain is either the sole or the dominant catalytically active domain.

About this Structure

1UW8 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site., Just VJ, Stevenson CE, Bowater L, Tanner A, Lawson DM, Bornemann S, J Biol Chem. 2004 May 7;279(19):19867-74. Epub 2004 Feb 10. PMID:14871895

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