1no3
From Proteopedia
(New page: 200px<br /><applet load="1no3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1no3, resolution 2.15Å" /> '''REFINED STRUCTURE OF...) |
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| - | [[Image:1no3.jpg|left|200px]]<br /><applet load="1no3" size=" | + | [[Image:1no3.jpg|left|200px]]<br /><applet load="1no3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1no3, resolution 2.15Å" /> | caption="1no3, resolution 2.15Å" /> | ||
'''REFINED STRUCTURE OF SOYBEAN LIPOXYGENASE-3 WITH 4-NITROCATECHOL AT 2.15 ANGSTROM RESOLUTION'''<br /> | '''REFINED STRUCTURE OF SOYBEAN LIPOXYGENASE-3 WITH 4-NITROCATECHOL AT 2.15 ANGSTROM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 4-Nitrocatechol (4NC) is a known inhibitor of lipoxygenase. This work | + | 4-Nitrocatechol (4NC) is a known inhibitor of lipoxygenase. This work presents the X-ray structure of soybean lipoxygenase-3 in complex with 4NC refined at 2.15 A resolution. The X-ray analysis shows 4NC near iron with partial occupancy, blocking access to Fe but not covalently bound to it. The two hydroxyl groups interact with the C-terminus (4-OH) and His523 ND1 (3-OH). The residues surrounding the iron cofactor, His518*, His523, His709, Ile857* COO(-) and water, form a trigonal bipyramid with the residues marked with asterisks in the axial positions. The water bound to iron and the presence of the inhibitor seem to be responsible for the rearrangements and changes in the geometry of the ligand distribution and confirm the displacement of His518 from iron coordination. A description of the catechol binding contributes to the understanding of lipoxygenase inhibition and the participation of its co-oxidative activity in the utilization of natural flavonoids. |
==About this Structure== | ==About this Structure== | ||
| - | 1NO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] with FE and 4NC as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1NO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=4NC:'>4NC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1BYT. Active as [http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NO3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lipoxygenase]] | [[Category: Lipoxygenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Borbulevych, O | + | [[Category: Borbulevych, O Y.]] |
[[Category: Jankun, J.]] | [[Category: Jankun, J.]] | ||
[[Category: Skrzypczak-Jankun, E.]] | [[Category: Skrzypczak-Jankun, E.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:10 2008'' |
Revision as of 12:08, 21 February 2008
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REFINED STRUCTURE OF SOYBEAN LIPOXYGENASE-3 WITH 4-NITROCATECHOL AT 2.15 ANGSTROM RESOLUTION
Overview
4-Nitrocatechol (4NC) is a known inhibitor of lipoxygenase. This work presents the X-ray structure of soybean lipoxygenase-3 in complex with 4NC refined at 2.15 A resolution. The X-ray analysis shows 4NC near iron with partial occupancy, blocking access to Fe but not covalently bound to it. The two hydroxyl groups interact with the C-terminus (4-OH) and His523 ND1 (3-OH). The residues surrounding the iron cofactor, His518*, His523, His709, Ile857* COO(-) and water, form a trigonal bipyramid with the residues marked with asterisks in the axial positions. The water bound to iron and the presence of the inhibitor seem to be responsible for the rearrangements and changes in the geometry of the ligand distribution and confirm the displacement of His518 from iron coordination. A description of the catechol binding contributes to the understanding of lipoxygenase inhibition and the participation of its co-oxidative activity in the utilization of natural flavonoids.
About this Structure
1NO3 is a Single protein structure of sequence from Glycine max with and as ligands. This structure supersedes the now removed PDB entry 1BYT. Active as Lipoxygenase, with EC number 1.13.11.12 Full crystallographic information is available from OCA.
Reference
Soybean lipoxygenase-3 in complex with 4-nitrocatechol., Skrzypczak-Jankun E, Borbulevych OY, Jankun J, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):613-5. Epub 2004, Feb 25. PMID:14993710
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