1vld
From Proteopedia
(New page: 200px<br /><applet load="1vld" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vld, resolution 2.35Å" /> '''Crystal Structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1vld.gif|left|200px]]<br /><applet load="1vld" size=" | + | [[Image:1vld.gif|left|200px]]<br /><applet load="1vld" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vld, resolution 2.35Å" /> | caption="1vld, resolution 2.35Å" /> | ||
'''Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici'''<br /> | '''Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1VLD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pelobacter_acidigallici Pelobacter acidigallici] with ACT, CA, MGD, 4MO and SF4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1VLD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pelobacter_acidigallici Pelobacter acidigallici] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MGD:'>MGD</scene>, <scene name='pdbligand=4MO:'>4MO</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLD OCA]. |
==Reference== | ==Reference== | ||
| Line 16: | Line 16: | ||
[[Category: Abt, D.]] | [[Category: Abt, D.]] | ||
[[Category: Einsle, O.]] | [[Category: Einsle, O.]] | ||
| - | [[Category: Kroneck, P | + | [[Category: Kroneck, P M.H.]] |
[[Category: Messerschmidt, A.]] | [[Category: Messerschmidt, A.]] | ||
[[Category: Niessen, H.]] | [[Category: Niessen, H.]] | ||
| Line 30: | Line 30: | ||
[[Category: molybdenum binding enzyme]] | [[Category: molybdenum binding enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:29 2008'' |
Revision as of 13:36, 21 February 2008
|
Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici
Overview
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.
About this Structure
1VLD is a Protein complex structure of sequences from Pelobacter acidigallici with , , , and as ligands. Active as Pyrogallol hydroxytransferase, with EC number 1.97.1.2 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:36:29 2008
