1bug
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1bug.gif|left|200px]]<br /><applet load="1bug" size=" | + | [[Image:1bug.gif|left|200px]]<br /><applet load="1bug" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bug, resolution 2.70Å" /> | caption="1bug, resolution 2.70Å" /> | ||
'''CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES)-INHIBITOR COMPLEX WITH PHENYLTHIOUREA (PTU)'''<br /> | '''CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES)-INHIBITOR COMPLEX WITH PHENYLTHIOUREA (PTU)'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1BUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ipomoea_batatas Ipomoea batatas] with CU and URS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Catechol_oxidase Catechol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.1 1.10.3.1] Known structural/functional Sites: <scene name='pdbsite=CU1:Binding Site For Cu A In Monomer A'>CU1</scene>, <scene name='pdbsite=CU2:Binding Site For Cu A In Monomer B'>CU2</scene>, <scene name='pdbsite=CU3:Binding Site For Cu B In Monomer A'>CU3</scene> and <scene name='pdbsite=CU4:Binding Site For Cu B In Monomer B'>CU4</scene>. Full crystallographic information is available from [http:// | + | 1BUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ipomoea_batatas Ipomoea batatas] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=URS:'>URS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Catechol_oxidase Catechol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.3.1 1.10.3.1] Known structural/functional Sites: <scene name='pdbsite=CU1:Binding+Site+For+Cu+A+In+Monomer+A'>CU1</scene>, <scene name='pdbsite=CU2:Binding+Site+For+Cu+A+In+Monomer+B'>CU2</scene>, <scene name='pdbsite=CU3:Binding+Site+For+Cu+B+In+Monomer+A'>CU3</scene> and <scene name='pdbsite=CU4:Binding+Site+For+Cu+B+In+Monomer+B'>CU4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUG OCA]. |
==Reference== | ==Reference== | ||
| Line 24: | Line 24: | ||
[[Category: ipomoea batatas]] | [[Category: ipomoea batatas]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:34:01 2008'' |
Revision as of 07:34, 3 February 2008
|
CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES)-INHIBITOR COMPLEX WITH PHENYLTHIOUREA (PTU)
Overview
Catechol oxidases are ubiquitous plant enzymes containing a dinuclear, copper center. In the wound-response mechanism of the plant they catalyze, the oxidation of a broad range of ortho-diphenols to the corresponding, o-quinones coupled with the reduction of oxygen to water. The crystal, structures of the enzyme from sweet potato in the resting dicupric, Cu(II)-Cu(II) state, the reduced dicuprous Cu(I)-Cu(I) form, and in, complex with the inhibitor phenylthiourea were analyzed. The catalytic, copper center is accommodated in a central four-helix-bundle located in a, hydrophobic pocket close to the surface. Both metal binding sites are, composed of three histidine ligands. His 109, ligated to the CuA site, is, covalently linked to Cys 92 by an unusual thioether bond. Based on, biochemical, spectroscopic and the presented structural data, a, catalytical mechanism is proposed in which one of the oxygen atoms of the, diphenolic substrate binds to CuB of the oxygenated enzyme.
About this Structure
1BUG is a Single protein structure of sequence from Ipomoea batatas with and as ligands. Active as Catechol oxidase, with EC number 1.10.3.1 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
Crystal structure of a plant catechol oxidase containing a dicopper center., Klabunde T, Eicken C, Sacchettini JC, Krebs B, Nat Struct Biol. 1998 Dec;5(12):1084-90. PMID:9846879
Page seeded by OCA on Sun Feb 3 09:34:01 2008
