1sdw
From Proteopedia
(New page: 200px<br /><applet load="1sdw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sdw, resolution 1.85Å" /> '''Reduced (Cu+) peptid...) |
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| - | [[Image:1sdw.gif|left|200px]]<br /><applet load="1sdw" size=" | + | [[Image:1sdw.gif|left|200px]]<br /><applet load="1sdw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1sdw, resolution 1.85Å" /> | caption="1sdw, resolution 1.85Å" /> | ||
'''Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen'''<br /> | '''Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Copper active sites play a major role in enzymatic activation of dioxygen. | + | Copper active sites play a major role in enzymatic activation of dioxygen. We trapped the copper-dioxygen complex in the enzyme peptidylglycine-alphahydroxylating monooxygenase (PHM) by freezing protein crystals that had been soaked with a slow substrate and ascorbate in the presence of oxygen. The x-ray crystal structure of this precatalytic complex, determined to 1.85-angstrom resolution, shows that oxygen binds to one of the coppers in the enzyme with an end-on geometry. Given this structure, it is likely that dioxygen is directly involved in the electron transfer and hydrogen abstraction steps of the PHM reaction. These insights may apply to other copper oxygen-activating enzymes, such as dopamine beta-monooxygenase, and to the design of biomimetic complexes. |
==About this Structure== | ==About this Structure== | ||
| - | 1SDW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CU, NI, OXY, IYT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] Full crystallographic information is available from [http:// | + | 1SDW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=OXY:'>OXY</scene>, <scene name='pdbligand=IYT:'>IYT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SDW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amzel, L | + | [[Category: Amzel, L M.]] |
| - | [[Category: Eipper, B | + | [[Category: Eipper, B A.]] |
| - | [[Category: Mains, R | + | [[Category: Mains, R E.]] |
| - | [[Category: Prigge, S | + | [[Category: Prigge, S T.]] |
[[Category: CU]] | [[Category: CU]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: beta jelly-roll]] | [[Category: beta jelly-roll]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:28 2008'' |
Revision as of 13:00, 21 February 2008
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Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen
Overview
Copper active sites play a major role in enzymatic activation of dioxygen. We trapped the copper-dioxygen complex in the enzyme peptidylglycine-alphahydroxylating monooxygenase (PHM) by freezing protein crystals that had been soaked with a slow substrate and ascorbate in the presence of oxygen. The x-ray crystal structure of this precatalytic complex, determined to 1.85-angstrom resolution, shows that oxygen binds to one of the coppers in the enzyme with an end-on geometry. Given this structure, it is likely that dioxygen is directly involved in the electron transfer and hydrogen abstraction steps of the PHM reaction. These insights may apply to other copper oxygen-activating enzymes, such as dopamine beta-monooxygenase, and to the design of biomimetic complexes.
About this Structure
1SDW is a Single protein structure of sequence from Rattus norvegicus with , , , and as ligands. Active as Peptidylglycine monooxygenase, with EC number 1.14.17.3 Full crystallographic information is available from OCA.
Reference
Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex., Prigge ST, Eipper BA, Mains RE, Amzel LM, Science. 2004 May 7;304(5672):864-7. PMID:15131304
Page seeded by OCA on Thu Feb 21 15:00:28 2008
Categories: Peptidylglycine monooxygenase | Rattus norvegicus | Single protein | Amzel, L M. | Eipper, B A. | Mains, R E. | Prigge, S T. | CU | GOL | IYT | NI | OXY | Beta jelly-roll
