1w7c

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[[Image:1w7c.gif|left|200px]]
 
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{{Structure
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==PPLO at 1.23 Angstroms==
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|PDB= 1w7c |SIZE=350|CAPTION= <scene name='initialview01'>1w7c</scene>, resolution 1.23&Aring;
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<StructureSection load='1w7c' size='340' side='right'caption='[[1w7c]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TPQ:'>TPQ</scene> and <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>
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<table><tr><td colspan='2'>[[1w7c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataella_pastoris Komagataella pastoris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7C FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Protein-lysine_6-oxidase Protein-lysine 6-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.13 1.4.3.13]
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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]] 1.23&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene></td></tr>
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}}
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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=1w7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7c OCA], [https://pdbe.org/1w7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7c RCSB], [https://www.ebi.ac.uk/pdbsum/1w7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7c ProSAT]</span></td></tr>
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</table>
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'''PPLO AT 1.23 ANGSTROMS'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q96X16_PICPA Q96X16_PICPA]
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== Evolutionary Conservation ==
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==Overview==
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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/w7/1w7c_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=1w7c 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 ==
The structure of Pichia pastoris lysyl oxidase (PPLO) in a new crystal form has been refined at 1.23 Angstrom resolution. PPLO, a copper amine oxidase (CuAO) with a 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor, differs from most other members of the CuAO enzyme family in having the ability to oxidize the side chain of lysine residues in a polypeptide. In the asymmetric unit of the crystals, the structure analysis has located residues 43-779 of the polypeptide chain, seven carbohydrate residues, the active-site Cu atom, an imidazole molecule bound at the active site, two buried Ca(2+) ions, five surface Mg(2+) ions, five surface Cl(-) ions and 1045 water molecules. The crystallographic residuals are R = 0.112 and R(free) = 0.146. The TPQ cofactor and several other active-site residues are poorly ordered, in contrast to the surrounding well ordered structure. A covalent cross-link is observed between two lysine residues, Lys778 and Lys66. The cross-link is likely to have been formed by the oxidation of Lys778 followed by a spontaneous reaction with Lys66. The link is modelled as dehydrolysinonorleucine.
The structure of Pichia pastoris lysyl oxidase (PPLO) in a new crystal form has been refined at 1.23 Angstrom resolution. PPLO, a copper amine oxidase (CuAO) with a 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor, differs from most other members of the CuAO enzyme family in having the ability to oxidize the side chain of lysine residues in a polypeptide. In the asymmetric unit of the crystals, the structure analysis has located residues 43-779 of the polypeptide chain, seven carbohydrate residues, the active-site Cu atom, an imidazole molecule bound at the active site, two buried Ca(2+) ions, five surface Mg(2+) ions, five surface Cl(-) ions and 1045 water molecules. The crystallographic residuals are R = 0.112 and R(free) = 0.146. The TPQ cofactor and several other active-site residues are poorly ordered, in contrast to the surrounding well ordered structure. A covalent cross-link is observed between two lysine residues, Lys778 and Lys66. The cross-link is likely to have been formed by the oxidation of Lys778 followed by a spontaneous reaction with Lys66. The link is modelled as dehydrolysinonorleucine.
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==About this Structure==
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The 1.23 Angstrom structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link.,Duff AP, Cohen AE, Ellis PJ, Hilmer K, Langley DB, Dooley DM, Freeman HC, Guss JM Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1073-84. Epub 2006, Aug 19. PMID:16929109<ref>PMID:16929109</ref>
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1W7C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7C OCA].
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==Reference==
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The 1.23 Angstrom structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link., Duff AP, Cohen AE, Ellis PJ, Hilmer K, Langley DB, Dooley DM, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1073-84. Epub 2006, Aug 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16929109 16929109]
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[[Category: Pichia pastoris]]
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[[Category: Protein-lysine 6-oxidase]]
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[[Category: Single protein]]
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[[Category: Cohen, A E.]]
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[[Category: Duff, A P.]]
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[[Category: Ellis, P J.]]
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[[Category: Guss, J M.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: CU]]
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[[Category: IMD]]
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[[Category: MG]]
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[[Category: NAG]]
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[[Category: TPQ]]
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[[Category: amne oxidase]]
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[[Category: copper]]
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[[Category: oxidase]]
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[[Category: oxidoreductase]]
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[[Category: quinoprotein]]
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[[Category: topaquinone enzyme]]
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[[Category: tpq]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:10 2008''
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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 1w7c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Komagataella pastoris]]
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[[Category: Large Structures]]
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[[Category: Cohen AE]]
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[[Category: Duff AP]]
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[[Category: Ellis PJ]]
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[[Category: Guss JM]]

Current revision

PPLO at 1.23 Angstroms

PDB ID 1w7c

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