1dos

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[[Image:1dos.gif|left|200px]]
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{{STRUCTURE_1dos| PDB=1dos | SCENE= }}
{{STRUCTURE_1dos| PDB=1dos | SCENE= }}
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'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''
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===STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE===
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==Overview==
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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.
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(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==
==About this Structure==
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[[Category: Glycolysis]]
[[Category: Glycolysis]]
[[Category: Lyase]]
[[Category: Lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:23:26 2008''

Revision as of 20:23, 30 June 2008

Image:1dos.png

Template:STRUCTURE 1dos

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

Template:ABSTRACT PUBMED 8836102

About this Structure

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

Reference

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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