2bl4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bl4.gif|left|200px]]<br /><applet load="2bl4" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2bl4.gif|left|200px]]
-
caption="2bl4, resolution 2.85&Aring;" />
+
 
-
'''LACTALDEHYDE:1,2-PROPANEDIOL OXIDOREDUCTASE OF ESCHERICHIA COLI'''<br />
+
{{Structure
 +
|PDB= 2bl4 |SIZE=350|CAPTION= <scene name='initialview01'>2bl4</scene>, resolution 2.85&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
 +
|ACTIVITY= [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]
 +
|GENE=
 +
}}
 +
 
 +
'''LACTALDEHYDE:1,2-PROPANEDIOL OXIDOREDUCTASE OF ESCHERICHIA COLI'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=NAD:'>NAD</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BL4 OCA].
+
2BL4 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=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://www.ncbi.nlm.nih.gov/pubmed/15995211 15995211]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Lactaldehyde reductase]]
[[Category: Lactaldehyde reductase]]
Line 29: Line 38:
[[Category: group iii dehydrogenase]]
[[Category: group iii dehydrogenase]]
[[Category: iron]]
[[Category: iron]]
-
[[Category: metalo-enzymes]]
+
[[Category: metalo-enzyme]]
[[Category: nad]]
[[Category: nad]]
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:55 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:03:21 2008''

Revision as of 14:03, 20 March 2008

Image:2bl4.gif


PDB ID 2bl4

Drag the structure with the mouse to rotate
, resolution 2.85Å
Sites:
Ligands: , and
Activity: Lactaldehyde reductase, with EC number 1.1.1.77
Coordinates: save as pdb, mmCIF, xml



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 located at the face of the cleft formed by the C-terminal domain, where the metal ion is tetrahedrally coordinated by three histidine residues (His200, His263, and His277) and an aspartate residue (Asp196). The glycine-rich turn formed by residues 96 to 98 and the following alpha-helix is part of the NAD(+) recognition locus common in dehydrogenases. Site-directed mutagenesis and enzyme kinetic assays were performed to assess the role of different residues in metal, cofactor, and substrate binding. In contrast to previous assumptions, the essential His267 residue does not interact with the metal ion. Asp39 appears to be the key residue for discriminating against NADP(+). Modeling L-1,2-propanediol in the active center resulted in a close approach of the C-1 hydroxyl of the substrate to C-4 of the nicotinamide ring, implying that there is a typical metal-dependent dehydrogenation catalytic mechanism.

About this Structure

2BL4 is a Single protein structure of sequence from Escherichia coli. 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 Thu Mar 20 16:03:21 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bl4"
Personal tools