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1yge

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(New page: 200px<br /><applet load="1yge" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yge, resolution 1.4&Aring;" /> '''LIPOXYGENASE-1 (SOYBE...)
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'''LIPOXYGENASE-1 (SOYBEAN) AT 100K'''<br />
'''LIPOXYGENASE-1 (SOYBEAN) AT 100K'''<br />
==Overview==
==Overview==
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Lipoxygenases, which are widely distributed among plant and animal, species, are Fe-containing dioxygenases that act on lipids containing, (Z,Z)-pentadiene moieties in the synthesis of compounds with a variety of, functions. Utilizing an improved strategy of data collection, low, temperature, and synchrotron radiation of short wavelength, the structure, of ferrous soybean lipoxygenase L-1, a single chain protein of 839 amino, acid residues, has been determined by X-ray crystallography to a, resolution of 1.4 A. The R-factor for the refined model is 19.7%. General, features of the protein structure were found to be consistent with the, results of prior crystallographic studies at lower (2.6 A) resolution. In, contrast to the prior studies, the binding of a water molecule to the, active site Fe was established. The octahedral coordination sphere of the, Fe also includes the side chains of His499, His504, His690, and Asn694 as, well as the terminal carboxylate of Ile839, which binds as a monodentate, ligand. Asn694 is involved in a number of labile polar interactions with, other protein groups, including an amide-aromatic hydrogen bond, and, appears to be a weak ligand. Several possible access routes for dioxygen, and fatty acids to the internal active site and substrate binding cavity, are described. The protein structure restricts access to the Fe site such, that the formation of an organo-Fe intermediate seems improbable., Structural restrictions pertinent to other proposed reaction, intermediates, such as planar pentadienyl and nonplanar allyl radicals, are also discussed.
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Lipoxygenases, which are widely distributed among plant and animal species, are Fe-containing dioxygenases that act on lipids containing (Z,Z)-pentadiene moieties in the synthesis of compounds with a variety of functions. Utilizing an improved strategy of data collection, low temperature, and synchrotron radiation of short wavelength, the structure of ferrous soybean lipoxygenase L-1, a single chain protein of 839 amino acid residues, has been determined by X-ray crystallography to a resolution of 1.4 A. The R-factor for the refined model is 19.7%. General features of the protein structure were found to be consistent with the results of prior crystallographic studies at lower (2.6 A) resolution. In contrast to the prior studies, the binding of a water molecule to the active site Fe was established. The octahedral coordination sphere of the Fe also includes the side chains of His499, His504, His690, and Asn694 as well as the terminal carboxylate of Ile839, which binds as a monodentate ligand. Asn694 is involved in a number of labile polar interactions with other protein groups, including an amide-aromatic hydrogen bond, and appears to be a weak ligand. Several possible access routes for dioxygen and fatty acids to the internal active site and substrate binding cavity are described. The protein structure restricts access to the Fe site such that the formation of an organo-Fe intermediate seems improbable. Structural restrictions pertinent to other proposed reaction intermediates, such as planar pentadienyl and nonplanar allyl radicals, are also discussed.
==About this Structure==
==About this Structure==
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1YGE 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YGE OCA].
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1YGE 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> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1YGE OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Axelrod, B.]]
[[Category: Axelrod, B.]]
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[[Category: Bolin, J.T.]]
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[[Category: Bolin, J T.]]
[[Category: Minor, W.]]
[[Category: Minor, W.]]
[[Category: Otwinowski, Z.]]
[[Category: Otwinowski, Z.]]
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[[Category: metalloprotein]]
[[Category: metalloprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:05 2008''

Revision as of 14:05, 21 February 2008

Image:1yge.jpg

1yge, resolution 1.4Å

Drag the structure with the mouse to rotate

LIPOXYGENASE-1 (SOYBEAN) AT 100K

Overview

Lipoxygenases, which are widely distributed among plant and animal species, are Fe-containing dioxygenases that act on lipids containing (Z,Z)-pentadiene moieties in the synthesis of compounds with a variety of functions. Utilizing an improved strategy of data collection, low temperature, and synchrotron radiation of short wavelength, the structure of ferrous soybean lipoxygenase L-1, a single chain protein of 839 amino acid residues, has been determined by X-ray crystallography to a resolution of 1.4 A. The R-factor for the refined model is 19.7%. General features of the protein structure were found to be consistent with the results of prior crystallographic studies at lower (2.6 A) resolution. In contrast to the prior studies, the binding of a water molecule to the active site Fe was established. The octahedral coordination sphere of the Fe also includes the side chains of His499, His504, His690, and Asn694 as well as the terminal carboxylate of Ile839, which binds as a monodentate ligand. Asn694 is involved in a number of labile polar interactions with other protein groups, including an amide-aromatic hydrogen bond, and appears to be a weak ligand. Several possible access routes for dioxygen and fatty acids to the internal active site and substrate binding cavity are described. The protein structure restricts access to the Fe site such that the formation of an organo-Fe intermediate seems improbable. Structural restrictions pertinent to other proposed reaction intermediates, such as planar pentadienyl and nonplanar allyl radicals, are also discussed.

About this Structure

1YGE is a Single protein structure of sequence from Glycine max with as ligand. Active as Lipoxygenase, with EC number 1.13.11.12 Full crystallographic information is available from OCA.

Reference

Crystal structure of soybean lipoxygenase L-1 at 1.4 A resolution., Minor W, Steczko J, Stec B, Otwinowski Z, Bolin JT, Walter R, Axelrod B, Biochemistry. 1996 Aug 20;35(33):10687-701. PMID:8718858

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