1fui
From Proteopedia
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| - | [[Image:1fui.gif|left|200px]] | + | [[Image:1fui.gif|left|200px]] |
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| - | '''L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1fui |SIZE=350|CAPTION= <scene name='initialview01'>1fui</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=FOC:FUCITOL'>FOC</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= FUCI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FUI is a [ | + | 1FUI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9367760 9367760] |
[[Category: Arabinose isomerase]] | [[Category: Arabinose isomerase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: l-fucose to l-fuculose conversion]] | [[Category: l-fucose to l-fuculose conversion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:14:08 2008'' |
Revision as of 09:14, 20 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | FUCI (Escherichia coli) | ||||||
| Activity: | Arabinose isomerase, with EC number 5.3.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 11:14:08 2008
