1opm

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[[Image:1opm.gif|left|200px]]<br /><applet load="1opm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1opm.gif|left|200px]]
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caption="1opm, resolution 2.1&Aring;" />
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'''OXIDIZED (CU2+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) WITH BOUND SUBSTRATE'''<br />
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{{Structure
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|PDB= 1opm |SIZE=350|CAPTION= <scene name='initialview01'>1opm</scene>, resolution 2.1&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=IYG:N-ALPHA-ACETYL-3,5-DIIODOTYROSYLGLYCINE'>IYG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''OXIDIZED (CU2+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) WITH BOUND SUBSTRATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OPM 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=AZI:'>AZI</scene>, <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=IYG:'>IYG</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=1OPM OCA].
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1OPM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPM OCA].
==Reference==
==Reference==
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Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Nat Struct Biol. 1999 Oct;6(10):976-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10504734 10504734]
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Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Nat Struct Biol. 1999 Oct;6(10):976-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10504734 10504734]
[[Category: Peptidylglycine monooxygenase]]
[[Category: Peptidylglycine monooxygenase]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:13:57 2008''

Revision as of 11:13, 20 March 2008

Image:1opm.gif


PDB ID 1opm

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands: , , , and
Activity: Peptidylglycine monooxygenase, with EC number 1.14.17.3
Coordinates: save as pdb, mmCIF, xml



OXIDIZED (CU2+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) WITH BOUND SUBSTRATE


Overview

Peptide amidation is a ubiquitous posttranslational modification of bioactive peptides. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzyme that catalyzes the first step of this reaction, is composed of two domains, each of which binds one copper atom. The coppers are held 11 A apart on either side of a solvent-filled interdomain cleft, and the PHM reaction requires electron transfer between these sites. A plausible mechanism for electron transfer might involve interdomain motion to decrease the distance between the copper atoms. Our experiments show that PHM catalytic core (PHMcc) is enzymatically active in the crystal phase, where interdomain motion is not possible. Instead, structures of two states relevant to catalysis indicate that water, substrate and active site residues may provide an electron transfer pathway that exists only during the PHM catalytic cycle.

About this Structure

1OPM is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase., Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM, Nat Struct Biol. 1999 Oct;6(10):976-83. PMID:10504734

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