4v4e: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v4e]] 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=1ti6 1ti6] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vlf 1vlf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4E FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v4e]] 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=1ti6 1ti6] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vlf 1vlf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4E FirstGlance]. <br> | ||
</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=BTT:BENZENE-1,2,4,5-TETROL'>BTT</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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=BTT:BENZENE-1,2,4,5-TETROL'>BTT</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=4v4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4e OCA], [https://pdbe.org/4v4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4e RCSB], [https://www.ebi.ac.uk/pdbsum/4v4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4e ProSAT]</span></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=4v4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4e OCA], [https://pdbe.org/4v4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4e RCSB], [https://www.ebi.ac.uk/pdbsum/4v4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 21:03, 20 September 2023
Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with inhibitor 1,2,4,5-tetrahydroxy-benzeneCrystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with inhibitor 1,2,4,5-tetrahydroxy-benzene
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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