1yip

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{{Seed}}
 
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[[Image:1yip.png|left|200px]]
 
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==Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form==
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The line below this paragraph, containing "STRUCTURE_1yip", creates the "Structure Box" on the page.
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<StructureSection load='1yip' size='340' side='right'caption='[[1yip]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1yip]] 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=1YIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIP FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.2&#8491;</td></tr>
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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></td></tr>
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{{STRUCTURE_1yip| PDB=1yip | SCENE= }}
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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=1yip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yip OCA], [https://pdbe.org/1yip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yip RCSB], [https://www.ebi.ac.uk/pdbsum/1yip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yip ProSAT]</span></td></tr>
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</table>
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== Function ==
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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/yi/1yip_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1yip 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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Many bioactive peptides require amidation of their carboxy terminus to exhibit full biological activity. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzyme that catalyzes the first of the two steps of this reaction, is composed of two domains, each of which binds one copper atom (CuH and CuM). The CuM site includes Met(314) and two His residues as ligands. Mutation of Met(314) to Ile inactivates PHM, but has only a minimal effect on the EXAFS spectrum of the oxidized enzyme, implying that it contributes only marginally to stabilization of the CuM site. To characterize the role of Met(314) as a CuM ligand, we determined the structure of the Met(314)Ile-PHM mutant. Since the mutant protein failed to crystallize in the conditions of the original wild-type protein, this structure determination required finding a new crystal form. The Met(314)Ile-PHM mutant structure confirms that the mutation does not abolish CuM binding to the enzyme, but causes other structural perturbations that affect the overall stability of the enzyme and the integrity of the CuH site. To eliminate possible effects of crystal contacts, we redetermined the structure of wt-PHM in the Met(314)Ile-PHM crystal form and showed that it does not differ from the structure of wild-type (wt)-PHM in the original crystals. Met(314)Ile-PHM was also shown to be less stable than wt-PHM by differential scanning calorimetry. Both structural and calorimetric studies point to a structural role for the CuM site, in addition to its established catalytic role.
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===Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form===
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The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role.,Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:16100265<ref>PMID:16100265</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 1yip" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16100265}}, adds the Publication Abstract to the page
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*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16100265 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16100265}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1YIP 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=1YIP OCA].
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==Reference==
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The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural role., Siebert X, Eipper BA, Mains RE, Prigge ST, Blackburn NJ, Amzel LM, Biophys J. 2005 Nov;89(5):3312-9. Epub 2005 Aug 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16100265 16100265]
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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: Blackburn NJ]]
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[[Category: Blackburn, N J.]]
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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: Siebert X]]
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[[Category: Siebert, X.]]
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[[Category: Ascorbate]]
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[[Category: Bioactive peptide activation]]
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[[Category: Copper]]
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[[Category: Monooxygenase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:25:28 2008''
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Current revision

Oxidized Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form

PDB ID 1yip

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