1dxy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dxy.gif|left|200px]]<br /><applet load="1dxy" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1dxy.gif|left|200px]]
-
caption="1dxy, resolution 1.86&Aring;" />
+
 
-
'''STRUCTURE OF D-2-HYDROXYISOCAPROATE DEHYDROGENASE'''<br />
+
{{Structure
 +
|PDB= 1dxy |SIZE=350|CAPTION= <scene name='initialview01'>1dxy</scene>, resolution 1.86&Aring;
 +
|SITE= <scene name='pdbsite=CAT:Active+Site'>CAT</scene>
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=COI:2-OXO-4-METHYLPENTANOIC ACID'>COI</scene>
 +
|ACTIVITY=
 +
|GENE= POTENTIAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1582 Lactobacillus casei])
 +
}}
 +
 
 +
'''STRUCTURE OF D-2-HYDROXYISOCAPROATE DEHYDROGENASE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1DXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=COI:'>COI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=CAT:Active+Site'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DXY OCA].
+
1DXY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_casei Lactobacillus casei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DXY OCA].
==Reference==
==Reference==
-
Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution., Dengler U, Niefind K, Kiess M, Schomburg D, J Mol Biol. 1997 Apr 4;267(3):640-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9126843 9126843]
+
Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution., Dengler U, Niefind K, Kiess M, Schomburg D, J Mol Biol. 1997 Apr 4;267(3):640-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9126843 9126843]
[[Category: Lactobacillus casei]]
[[Category: Lactobacillus casei]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 24: Line 33:
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:42 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:46:14 2008''

Revision as of 08:46, 20 March 2008


PDB ID 1dxy

Drag the structure with the mouse to rotate
, resolution 1.86Å
Sites:
Ligands: , and
Gene: POTENTIAL (Lactobacillus casei)
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF D-2-HYDROXYISOCAPROATE DEHYDROGENASE


Overview

D-2-hydroxyisocaproate dehydrogenase (D-HicDH) from Lactobacillus casei is a homodimer with 333 amino acids and a molecular mass of 37 kDa per subunit. The enzyme belongs to the protein family of NAD+-dependent D-2-hydroxycarboxylate dehydrogenases and within this family to the subgroup of D-lactate dehydrogenases (D-LDHs). Compared with other D-LDHs D-HicDH is characterized by a very low specificity regarding size and chemical constitution of the accepted D-2-hydroxycarboxylates. Hexagonal crystals of recombinant D-HicDH in the presence of NAD+ and 2-oxoisocaproate (4-methyl-2-oxopentanoate) were grown with ammonium sulphate as precipitating agent. The structure of these crystals was solved by molecular replacement and refined to a final R-factor of 19.6% for all measured X-ray reflections in the resolution range (infinity to 1.86 A). Both NAD+ and 2-oxoisocaproate were identified in the electron density map; binding of the latter in the active site, however, competes with a sulphate ion, which is also defined by electron density. Additionally the final model contains 182 water molecules and a second sulphate ion. The binding of both an in vitro substrate and the natural cosubstrate in the active site provides substantial insight into the catalytic mechanism and allows us to assess previously published active site models for this enzyme family, in particular the two most controversial points, the role of the conserved Arg234 and substrate binding. Furthermore the overall topology and details of the D-HicDH structure are described, discussed against the background of homologous structures and compared with one closely and one distantly related protein.

About this Structure

1DXY is a Single protein structure of sequence from Lactobacillus casei. Full crystallographic information is available from OCA.

Reference

Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution., Dengler U, Niefind K, Kiess M, Schomburg D, J Mol Biol. 1997 Apr 4;267(3):640-60. PMID:9126843

Page seeded by OCA on Thu Mar 20 10:46:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools