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1qpa

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(New page: 200px<br /> <applet load="1qpa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qpa, resolution 1.80&Aring;" /> '''LIGNIN PEROXIDASE I...)
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[[Image:1qpa.gif|left|200px]]<br />
 
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<applet load="1qpa" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qpa, resolution 1.80&Aring;" />
 
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'''LIGNIN PEROXIDASE ISOZYME LIP4.65 (PI 4.65)'''<br />
 
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==Overview==
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==LIGNIN PEROXIDASE ISOZYME LIP4.65 (PI 4.65)==
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The crystal structure of lignin peroxidase (LiP) from the white rot fungus, Phanerochaete chrysosporium was refined to an R-factor of 16.2 % utilizing, synchrotron data in the resolution range from 10 to 1.7 A. The final model, comprises all 343 amino acid residues, 370 water molecules, the heme, four, carbohydrates, and two calcium ions. Lignin peroxidase shows the typical, peroxidase fold and the heme has a close environment as found in other, peroxidases. During refinement of the LiP model an unprecedented, modification of an amino acid was recognized. The surface residue, tryptophan 171 in LiP is stereospecifically hydroxylated at the Cbeta atom, due to an autocatalytic process. We propose that during the catalytic, cycle of LiP a transient radical at Trp171 occurs that is different ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10024453 (full description)]]
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<StructureSection load='1qpa' size='340' side='right'caption='[[1qpa]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qpa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QPA FirstGlance]. <br>
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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]] 1.8&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HTR:BETA-HYDROXYTRYPTOPHANE'>HTR</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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=1qpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpa OCA], [https://pdbe.org/1qpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qpa RCSB], [https://www.ebi.ac.uk/pdbsum/1qpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIG4_PHACH LIG4_PHACH] Depolymerization of lignin. Catalyzes the C(alpha)-C(beta) cleavage of the propyl side chains of lignin.
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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/qp/1qpa_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=1qpa ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1QPA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with NAG, MAN, CA and HEM as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QPA OCA]].
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*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
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*[[Lignin peroxidase|Lignin peroxidase]]
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==Reference==
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__TOC__
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The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle., Choinowski T, Blodig W, Winterhalter KH, Piontek K, J Mol Biol. 1999 Feb 26;286(3):809-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10024453 10024453]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Choinowski, T.H.]]
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[[Category: Phanerodontia chrysosporium]]
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[[Category: Piontek, K.]]
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[[Category: Choinowski TH]]
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[[Category: CA]]
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[[Category: Piontek K]]
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[[Category: HEM]]
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[[Category: MAN]]
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[[Category: NAG]]
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[[Category: glycoprotein]]
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[[Category: heme]]
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[[Category: lignin degradation]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:02:02 2007''
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Current revision

LIGNIN PEROXIDASE ISOZYME LIP4.65 (PI 4.65)

PDB ID 1qpa

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