2bl4
From Proteopedia
(New page: 200px<br /> <applet load="2bl4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bl4, resolution 2.85Å" /> '''LACTALDEHYDE:1,2-PR...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2BL4 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 FE2, CL and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.77 1.1.1.77]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BL4 OCA]]. | + | 2BL4 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 FE2, CL and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Lactaldehyde_reductase Lactaldehyde reductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.77 1.1.1.77]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BL4 OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli., Montella C, Bellsolell L, Perez-Luque R, Badia J, Baldoma L, Coll M, Aguilar J, J Bacteriol. 2005 Jul;187(14):4957-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15995211 15995211] | Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli., Montella C, Bellsolell L, Perez-Luque R, Badia J, Baldoma L, Coll M, Aguilar J, J Bacteriol. 2005 Jul;187(14):4957-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15995211 15995211] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Lactaldehyde reductase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Aguilar, J.]] | [[Category: Aguilar, J.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:52:03 2007'' |
Revision as of 11:47, 30 October 2007
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LACTALDEHYDE:1,2-PROPANEDIOL OXIDOREDUCTASE OF ESCHERICHIA COLI
Overview
The FucO protein, a member of the group III "iron-activated", dehydrogenases, catalyzes the interconversion between L-lactaldehyde and, L-1,2-propanediol in Escherichia coli. The three-dimensional structure of, FucO in a complex with NAD(+) was solved, and the presence of iron in the, crystals was confirmed by X-ray fluorescence. The FucO structure presented, here is the first structure for a member of the group III bacterial, dehydrogenases shown experimentally to contain iron. FucO forms a dimer, in which each monomer folds into an alpha/beta dinucleotide-binding, N-terminal domain and an all-alpha-helix C-terminal domain that are, separated by a deep cleft. The dimer is formed by the swapping (between, monomers) of the first chain of the beta-sheet. The binding site for, Fe(2+) is ... [(full description)]
About this Structure
2BL4 is a [Single protein] structure of sequence from [Escherichia coli] with FE2, CL and NAD as [ligands]. Active as [Lactaldehyde reductase], with EC number [1.1.1.77]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of an iron-dependent group III dehydrogenase that interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli., Montella C, Bellsolell L, Perez-Luque R, Badia J, Baldoma L, Coll M, Aguilar J, J Bacteriol. 2005 Jul;187(14):4957-66. PMID:15995211
Page seeded by OCA on Tue Oct 30 13:52:03 2007
Categories: Escherichia coli | Lactaldehyde reductase | Single protein | Aguilar, J. | Badia, J. | Baldoma, L. | Bellsolell, L. | Coll, M. | Montella, C. | Perez-Luque, R. | CL | FE2 | NAD | Dinucleotide cofactor specificity | Fuco | Fucose metabolism | Group iii dehydrogenase | Iron | Metalo-enzymes | Nad | Oxidoreductase
