1bg6: Difference between revisions

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[[Image:1bg6.~~jpg~~|left|200px]]

[[Image:1bg6.png|left|200px]]

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

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

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_9665174}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9665174 is the PubMed ID number.

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==About this Structure==

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[[Category: Rice, D W.]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:28:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:05:35 2008''

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-[[Image:1bg6.jpg|left|200px]]
+{{Seed}}
+[[Image:1bg6.png|left|200px]]
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 {{STRUCTURE_1bg6|  PDB=1bg6  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE FROM ARTHROBACTER SP. STRAIN 1C'''
+===CRYSTAL STRUCTURE OF THE N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE FROM ARTHROBACTER SP. STRAIN 1C===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9665174}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9665174 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9665174}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Rice, D W.]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:28:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:05:35 2008''