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| - | ==Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici==
| + | #REDIRECT [[4v4c]] This PDB entry is obsolete and replaced by 4v4c |
| - | <StructureSection load='1vld' size='340' side='right' caption='[[1vld]], [[Resolution|resolution]] 2.35Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[1vld]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Pelobacter_acidigallici Pelobacter acidigallici]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VLD FirstGlance]. <br>
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| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4MO:MOLYBDENUM(IV)+ION'>4MO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene><br>
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| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ti2|1ti2]], [[1ti4|1ti4]], [[1ti6|1ti6]], [[1vle|1vle]], [[1vlf|1vlf]]</td></tr>
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| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyrogallol_hydroxytransferase Pyrogallol hydroxytransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.97.1.2 1.97.1.2] </span></td></tr>
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| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vld OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1vld RCSB], [http://www.ebi.ac.uk/pdbsum/1vld PDBsum]</span></td></tr>
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| - | <table>
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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/vl/1vld_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/chain_selection.php?pdb_ID=2ata 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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| - | The Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter acidigallici catalyzes the conversion of pyrogallol to phloroglucinol. Such trihydroxybenzenes and their derivatives represent important building blocks of plant polymers. None of the transferred hydroxyl groups originates from water during transhydroxylation; instead a cosubstrate, such as 1,2,3,5-tetrahydroxybenzene, is used in a reaction without apparent electron transfer. Here, we report on the crystal structure of the enzyme in the reduced Mo(IV) state, which we solved by single anomalous-diffraction technique. It represents the largest structure (1,149 amino acid residues per molecule, 12 independent molecules per unit cell), which has been solved so far by single anomalous-diffraction technique. Tranhydroxylase is a heterodimer, with the active Mo-molybdopterin guanine dinucleotide (MGD)(2) site in the alpha-subunit, and three [4Fe-4S] centers in the beta-subunit. The latter subunit carries a seven-stranded, mainly antiparallel beta-barrel domain. We propose a scheme for the transhydroxylation reaction based on 3D structures of complexes of the enzyme with various polyphenols serving either as substrate or inhibitor.
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| - | Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols.,Messerschmidt A, Niessen H, Abt D, Einsle O, Schink B, Kroneck PM Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11571-6. Epub 2004 Jul 29. PMID:15284442<ref>PMID:15284442</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </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: Pelobacter acidigallici]]
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| - | [[Category: Pyrogallol hydroxytransferase]]
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| - | [[Category: Abt, D.]]
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| - | [[Category: Einsle, O.]]
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| - | [[Category: Kroneck, P M.H.]]
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| - | [[Category: Messerschmidt, A.]]
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| - | [[Category: Niessen, H.]]
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| - | [[Category: Schink, B.]]
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| - | [[Category: 4fe-4s-cluster]]
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| - | [[Category: Dmso-reductase family]]
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| - | [[Category: Mgd-cofactor]]
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| - | [[Category: Molybdenum binding enzyme]]
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| - | [[Category: Oxidoreductase]]
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