1sdw

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[[Image:1sdw.gif|left|200px]]
 
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{{Structure
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==Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen==
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|PDB= 1sdw |SIZE=350|CAPTION= <scene name='initialview01'>1sdw</scene>, resolution 1.85&Aring;
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<StructureSection load='1sdw' size='340' side='right'caption='[[1sdw]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IYT:N-ALPHA-ACETYL-3,5-DIIODOTYROSYL-D-THREONINE'>IYT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>
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<table><tr><td colspan='2'>[[1sdw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SDW FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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|GENE= PAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IYT:N-ALPHA-ACETYL-3,5-DIIODOTYROSYL-D-THREONINE'>IYT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sdw OCA], [https://pdbe.org/1sdw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sdw RCSB], [https://www.ebi.ac.uk/pdbsum/1sdw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sdw ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1phm|1phm]], [[1opm|1opm]], [[3phm|3phm]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sdw OCA], [http://www.ebi.ac.uk/pdbsum/1sdw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sdw RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sd/1sdw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sdw ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen'''
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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<ref>PMID:15131304</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1sdw" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1SDW 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=1SDW OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15131304 15131304]
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[[Category: Peptidylglycine monooxygenase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Amzel LM]]
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[[Category: Amzel, L M.]]
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[[Category: Eipper BA]]
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[[Category: Eipper, B A.]]
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[[Category: Mains RE]]
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[[Category: Mains, R E.]]
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[[Category: Prigge ST]]
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[[Category: Prigge, S T.]]
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[[Category: beta jelly-roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:40:43 2008''
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Current revision

Reduced (Cu+) peptidylglycine alpha-hydroxylating monooxygenase with bound peptide and dioxygen

PDB ID 1sdw

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