1opm

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[[Image:1opm.gif|left|200px]]
[[Image:1opm.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1opm |SIZE=350|CAPTION= <scene name='initialview01'>1opm</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1opm", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IYG:N-ALPHA-ACETYL-3,5-DIIODOTYROSYLGLYCINE'>IYG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1opm| PDB=1opm | SCENE= }}
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|RELATEDENTRY=[[1phm|1PHM]], [[3phm|3PHM]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1opm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opm OCA], [http://www.ebi.ac.uk/pdbsum/1opm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1opm RCSB]</span>
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}}
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'''OXIDIZED (CU2+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) WITH BOUND SUBSTRATE'''
'''OXIDIZED (CU2+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM) WITH BOUND SUBSTRATE'''
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[[Category: Amzel, L M.]]
[[Category: Amzel, L M.]]
[[Category: Prigge, S T.]]
[[Category: Prigge, S T.]]
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[[Category: ascorbate]]
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[[Category: Ascorbate]]
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[[Category: bioactive peptide activation]]
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[[Category: Bioactive peptide activation]]
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[[Category: copper]]
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[[Category: Copper]]
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[[Category: monooxygenase]]
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[[Category: Monooxygenase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:08:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:35 2008''
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Revision as of 01:08, 3 May 2008

Image:1opm.gif

Template:STRUCTURE 1opm

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 Page seeded by OCA on Sat May 3 04:08:02 2008

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