2hg2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hg2.jpg|left|200px]]<br /><applet load="2hg2" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2hg2.jpg|left|200px]]
-
caption="2hg2, resolution 2.2&Aring;" />
+
 
-
'''Structure of Lactaldehyde Dehydrogenase'''<br />
+
{{Structure
 +
|PDB= 2hg2 |SIZE=350|CAPTION= <scene name='initialview01'>2hg2</scene>, resolution 2.2&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
 +
|ACTIVITY=
 +
|GENE= aldA, ald ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
 +
}}
 +
 
 +
'''Structure of Lactaldehyde Dehydrogenase'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2HG2 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HG2 OCA].
+
2HG2 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=2HG2 OCA].
==Reference==
==Reference==
-
Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity., Di Costanzo L, Gomez GA, Christianson DW, J Mol Biol. 2007 Feb 16;366(2):481-93. Epub 2006 Nov 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17173928 17173928]
+
Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity., Di Costanzo L, Gomez GA, Christianson DW, J Mol Biol. 2007 Feb 16;366(2):481-93. Epub 2006 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17173928 17173928]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 20: Line 29:
[[Category: nad dependent]]
[[Category: nad dependent]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:38 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:16:38 2008''

Revision as of 15:16, 20 March 2008


PDB ID 2hg2

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands:
Gene: aldA, ald (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



Structure of Lactaldehyde Dehydrogenase


Overview

Aldehyde dehydrogenases catalyze the oxidation of aldehyde substrates to the corresponding carboxylic acids. Lactaldehyde dehydrogenase from Escherichia coli (aldA gene product, P25553) is an NAD(+)-dependent enzyme implicated in the metabolism of l-fucose and l-rhamnose. During the heterologous expression and purification of taxadiene synthase from the Pacific yew, lactaldehyde dehydrogenase from E. coli was identified as a minor (</=5%) side-product subsequent to its unexpected crystallization. Accordingly, we now report the serendipitous crystal structure determination of unliganded lactaldehyde dehydrogenase from E. coli determined by the technique of multiple isomorphous replacement using anomalous scattering at 2.2 A resolution. Additionally, we report the crystal structure of the ternary enzyme complex with products lactate and NADH at 2.1 A resolution, and the crystal structure of the enzyme complex with NADPH at 2.7 A resolution. The structure of the ternary complex reveals that the nicotinamide ring of the cofactor is disordered between two conformations: one with the ring positioned in the active site in the so-called hydrolysis conformation, and another with the ring extended out of the active site into the solvent region, designated the out conformation. This represents the first crystal structure of an aldehyde dehydrogenase-product complex. The active site pocket in which lactate binds is more constricted than that of medium-chain dehydrogenases such as the YdcW gene product of E. coli. The structure of the binary complex with NADPH reveals the first view of the structural basis of specificity for NADH: the negatively charged carboxylate group of E179 destabilizes the binding of the 2'-phosphate group of NADPH sterically and electrostatically, thereby accounting for the lack of enzyme activity with this cofactor.

About this Structure

2HG2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity., Di Costanzo L, Gomez GA, Christianson DW, J Mol Biol. 2007 Feb 16;366(2):481-93. Epub 2006 Nov 10. PMID:17173928

Page seeded by OCA on Thu Mar 20 17:16:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools