1ti4: Difference between revisions

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[[Image:1ti4.gif|left|200px]]<br /><applet load="1ti4" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ti4.gif|left|200px]]<br /><applet load="1ti4" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ti4, resolution 2.20Å" />

'''Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with pyrogallol'''<br />

==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.

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==

1TI4 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 CA, MGD, 4MO, SF4 and PYG 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1TI4 OCA].

1TI4 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=CA:'>CA</scene>, <scene name='pdbligand=MGD:'>MGD</scene>, <scene name='pdbligand=4MO:'>4MO</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=PYG:'>PYG</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=1TI4 OCA].

==Reference==

Line 16:

[[Category: Abt, D.]]

[[Category: Einsle, O.]]

[[Category: Kroneck, P.M.H.]]

[[Category: Kroneck, P M.H.]]

[[Category: Messerschmidt, A.]]

[[Category: Niessen, H.]]

Line 31:

[[Category: molybdenum binding enzyme]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:45 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ti4.gif|left|200px]]<br /><applet load="1ti4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ti4.gif|left|200px]]<br /><applet load="1ti4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ti4, resolution 2.20&Aring;" />
 '''Crystal Structure of Pyrogallol-Phloroglucinol Transhydroxylase from Pelobacter acidigallici complexed with pyrogallol'''<br />
 ==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.
+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==
-TI4 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 CA, MGD, 4MO, SF4 and PYG 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TI4 OCA].
+TI4 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=CA:'>CA</scene>, <scene name='pdbligand=MGD:'>MGD</scene>, <scene name='pdbligand=4MO:'>4MO</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=PYG:'>PYG</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=1TI4 OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Abt, D.]]
 [[Category: Einsle, O.]]
-[[Category: Kroneck, P.M.H.]]
+[[Category: Kroneck, P M.H.]]
 [[Category: Messerschmidt, A.]]
 [[Category: Niessen, H.]]
@@ Line 31: / Line 31: @@
 [[Category: molybdenum binding enzyme]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:17:07 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:45 2008''