1ad3: Difference between revisions

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[[Image:1ad3.~~gif~~|left|200px]]

[[Image:1ad3.png|left|200px]]

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~~'''~~CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE~~'''~~

===CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE===

~~==Overview==~~

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The ~~first structure of an aldehyde dehydrogenase~~ (~~ALDH) is described~~ at 2.~~6 A resolution~~. ~~Each subunit of the dimeric enzyme contains an NAD-binding domain~~, ~~a catalytic domain and a bridging domain. At~~ the ~~interface of these domains is a 15 A long funnel-shaped passage with a 6 x 12 A opening leading to a putative catalytic pocket~~. ~~A new mode of NAD binding, which differs substantially from the classic beta~~-~~alpha~~-beta binding mode associated with the 'Rossmann fold', is observed which we term the beta-alpha,beta mode. Sequence comparisons of the class 3 ALDH with other ALDHs indicate a similar polypeptide fold, novel NAD-binding mode and catalytic site for this family. A mechanism for enzymatic specificity and activity is postulated.

The line below this paragraph, {{ABSTRACT_PUBMED_9095201}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9095201 is the PubMed ID number.

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==About this Structure==

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[[Category: Nadp]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 10~~:06:59 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:36:20 2008''

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-[[Image:1ad3.gif|left|200px]]
+{{Seed}}
+[[Image:1ad3.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ad3|  PDB=1ad3  |  SCENE=  }}
-'''CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE'''
+===CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE===
-==Overview==
+<!--
-The first structure of an aldehyde dehydrogenase (ALDH) is described at 2.6 A resolution. Each subunit of the dimeric enzyme contains an NAD-binding domain, a catalytic domain and a bridging domain. At the interface of these domains is a 15 A long funnel-shaped passage with a 6 x 12 A opening leading to a putative catalytic pocket. A new mode of NAD binding, which differs substantially from the classic beta-alpha-beta binding mode associated with the 'Rossmann fold', is observed which we term the beta-alpha,beta mode. Sequence comparisons of the class 3 ALDH with other ALDHs indicate a similar polypeptide fold, novel NAD-binding mode and catalytic site for this family. A mechanism for enzymatic specificity and activity is postulated.
+The line below this paragraph, {{ABSTRACT_PUBMED_9095201}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9095201 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9095201}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Nadp]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:06:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:36:20 2008''