1bg6

From Proteopedia

(Difference between revisions)

Revision as of 04:33, 25 December 2014

CRYSTAL STRUCTURE OF THE N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE FROM ARTHROBACTER SP. STRAIN 1C

Structural highlights

1bg6 is a 1 chain structure with sequence from Arthrobacter sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	ODH (Arthrobacter sp.)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ODH_ARTSC] In the forward direction acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. In the reverse direction, the enzyme also acts on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Opine dehydrogenases catalyze the NAD(P)H-dependent reversible reaction to form opines that contain two asymmetric centers exhibiting either (L,L) or (D,L) stereochemistry. The first structure of a (D,L) superfamily member, N-(1-D-carboxylethyl)-L-norvaline dehydrogenase (CENDH) from Arthrobacter sp. strain 1C, has been determined at 1.8 A resolution and the location of the bound nucleotide coenzyme has been identified. Six conserved residues cluster in the cleft between the enzyme's two domains, close to the nucleotide binding site, and are presumed to define the enzyme's catalytic machinery. Conservation of a His-Asp pair as part of this cluster suggests that the enzyme mechanism is related to the 2-hydroxy acid dehydrogenases. The pattern of sequence conservation and substitution between members of this enzyme family has permitted the tentative location of the residues that define their differential substrate specificities.

Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase.,Britton KL, Asano Y, Rice DW Nat Struct Biol. 1998 Jul;5(7):593-601. PMID:9665174^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Britton KL, Asano Y, Rice DW. Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase. Nat Struct Biol. 1998 Jul;5(7):593-601. PMID:9665174 doi:10.1038/854

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bg6"

Categories: Arthrobacter sp | Asano, Y | Britton, K L | Rice, D W | Oxidoreductase

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bg6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bg6 RCSB], [http://www.ebi.ac.uk/pdbsum/1bg6 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ODH_ARTSC ODH_ARTSC]] In the forward direction acts also on secondary amine dicarboxylates such as N-(1-carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. In the reverse direction, the enzyme also acts on neutral amino acids as an amino donor. They include L-amino acids such as 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, phenylalanine, leucine and alanine.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1bg6

From Proteopedia

Revision as of 04:33, 25 December 2014

CRYSTAL STRUCTURE OF THE N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE FROM ARTHROBACTER SP. STRAIN 1C

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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