1ad3: Difference between revisions

Revision as of 16:36, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ad3.png

Template:STRUCTURE 1ad3

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

Template:ABSTRACT PUBMED 9095201

About this StructureAbout this Structure

1AD3 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold., Liu ZJ, Sun YJ, Rose J, Chung YJ, Hsiao CD, Chang WR, Kuo I, Perozich J, Lindahl R, Hempel J, Wang BC, Nat Struct Biol. 1997 Apr;4(4):317-26. PMID:9095201

Page seeded by OCA on Mon Jun 30 16:36:20 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[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''