4v4c: Difference between revisions
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<StructureSection load='4v4c' size='340' side='right'caption='[[4v4c]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='4v4c' size='340' side='right'caption='[[4v4c]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v4c]] is a 24 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4v4c]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Pelobacter_acidigallici Pelobacter acidigallici]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ti2 1ti2] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vld 1vld]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><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 | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4v4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4c OCA], [https://pdbe.org/4v4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4c RCSB], [https://www.ebi.ac.uk/pdbsum/4v4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4c ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PGTL_PELAC PGTL_PELAC] Isomerisation of pyrogallol to phloroglucin. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pelobacter acidigallici]] | [[Category: Pelobacter acidigallici]] | ||
[[Category: Abt D]] | |||
[[Category: Abt | [[Category: Einsle O]] | ||
[[Category: Einsle | [[Category: Kroneck PMH]] | ||
[[Category: Kroneck | [[Category: Messerschmidt A]] | ||
[[Category: Messerschmidt | [[Category: Niessen H]] | ||
[[Category: Niessen | [[Category: Schink B]] | ||
[[Category: Schink | |||
Revision as of 11:03, 29 March 2023
Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigalliciCrystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici
Structural highlights
FunctionPGTL_PELAC Isomerisation of pyrogallol to phloroglucin. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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