1dxy
From Proteopedia
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| - | [[Image:1dxy.gif|left|200px]]<br /><applet load="1dxy" size=" | + | [[Image:1dxy.gif|left|200px]]<br /><applet load="1dxy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dxy, resolution 1.86Å" /> | caption="1dxy, resolution 1.86Å" /> | ||
'''STRUCTURE OF D-2-HYDROXYISOCAPROATE DEHYDROGENASE'''<br /> | '''STRUCTURE OF D-2-HYDROXYISOCAPROATE DEHYDROGENASE'''<br /> | ||
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==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 SO4, NAD and COI 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:35:58 2008'' |
Revision as of 07:35, 3 February 2008
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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 with , and as ligands. Known structural/functional Site: . 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
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