1dos: Difference between revisions

Revision as of 23:23, 30 June 2008

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File:1dos.png

Template:STRUCTURE 1dos

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASESTRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

Template:ABSTRACT PUBMED 8836102

About this StructureAbout this Structure

1DOS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase., Blom NS, Tetreault S, Coulombe R, Sygusch J, Nat Struct Biol. 1996 Oct;3(10):856-62. PMID:8836102

Page seeded by OCA on Mon Jun 30 23:23:26 2008

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-'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''
+===STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE===
-==Overview==
+<!--
-The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 A apart; the exclusivity is mediated by a conformational transition involving side-chain rotations by chelating histidine residues. A binding site for K+ and NH4+ activators was found near the beta-barrel centre. Although Class I and Class II aldolases catalyse identical reactions, their active sites do not share common amino acid residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct.
+The line below this paragraph, {{ABSTRACT_PUBMED_8836102}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8836102 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8836102}}
 ==About this Structure==
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 [[Category: Glycolysis]]
 [[Category: Lyase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:05:39 2008''
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