1fui
From Proteopedia
(New page: 200px<br /><applet load="1fui" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fui, resolution 2.50Å" /> '''L-FUCOSE ISOMERASE F...) |
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| - | [[Image:1fui.gif|left|200px]]<br /><applet load="1fui" size=" | + | [[Image:1fui.gif|left|200px]]<br /><applet load="1fui" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fui, resolution 2.50Å" /> | caption="1fui, resolution 2.50Å" /> | ||
'''L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI'''<br /> | '''L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of L-fucose isomerase from Escherichia | + | The three-dimensional structure of L-fucose isomerase from Escherichia coli has been determined by X-ray crystallography at 2.5 A resolution. This ketol isomerase converts the aldose L-fucose into the corresponding ketose L-fuculose using Mn2+ as a cofactor. Being a hexamer with 64,976 Da per subunit, L-fucose isomerase is the largest structurally known ketol isomerase. The enzyme shows neither sequence nor structural similarity with other ketol isomerases. The hexamer obeys D3 symmetry and forms the crystallographic asymmetric unit. The strict and favorably oriented local symmetry allowed for a computational phase extension from 7.3 A to 2.5 A resolution. The structure was solved with an L-fucitol molecule bound to the catalytic center such that the hydroxyl groups at positions 1 and 2 are ligands of the manganese ion. Most likely, L-fucitol mimics a bound L-fucose molecule in its open chain form. The protein environment suggests strongly that the reaction belongs to the ene-diol type. |
==About this Structure== | ==About this Structure== | ||
| - | 1FUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN, SO4 and FOC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arabinose_isomerase Arabinose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.3 5.3.1.3] Full crystallographic information is available from [http:// | + | 1FUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FOC:'>FOC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arabinose_isomerase Arabinose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.3 5.3.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
| - | [[Category: Seemann, J | + | [[Category: Seemann, J E.]] |
[[Category: FOC]] | [[Category: FOC]] | ||
[[Category: MN]] | [[Category: MN]] | ||
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[[Category: l-fucose to l-fuculose conversion]] | [[Category: l-fucose to l-fuculose conversion]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:44 2008'' |
Revision as of 10:42, 21 February 2008
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L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI
Overview
The three-dimensional structure of L-fucose isomerase from Escherichia coli has been determined by X-ray crystallography at 2.5 A resolution. This ketol isomerase converts the aldose L-fucose into the corresponding ketose L-fuculose using Mn2+ as a cofactor. Being a hexamer with 64,976 Da per subunit, L-fucose isomerase is the largest structurally known ketol isomerase. The enzyme shows neither sequence nor structural similarity with other ketol isomerases. The hexamer obeys D3 symmetry and forms the crystallographic asymmetric unit. The strict and favorably oriented local symmetry allowed for a computational phase extension from 7.3 A to 2.5 A resolution. The structure was solved with an L-fucitol molecule bound to the catalytic center such that the hydroxyl groups at positions 1 and 2 are ligands of the manganese ion. Most likely, L-fucitol mimics a bound L-fucose molecule in its open chain form. The protein environment suggests strongly that the reaction belongs to the ene-diol type.
About this Structure
1FUI is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Arabinose isomerase, with EC number 5.3.1.3 Full crystallographic information is available from OCA.
Reference
Structure and mechanism of L-fucose isomerase from Escherichia coli., Seemann JE, Schulz GE, J Mol Biol. 1997 Oct 17;273(1):256-68. PMID:9367760
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