1dos: Difference between revisions

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[[Image:1dos.gif|left|200px]]
[[Image:1dos.gif|left|200px]]


{{Structure
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|PDB= 1dos |SIZE=350|CAPTION= <scene name='initialview01'>1dos</scene>, resolution 1.67&Aring;
The line below this paragraph, containing "STRUCTURE_1dos", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
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|DOMAIN=
{{STRUCTURE_1dos| PDB=1dos  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dos OCA], [http://www.ebi.ac.uk/pdbsum/1dos PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dos RCSB]</span>
}}


'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''
'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''
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[[Category: Sygusch, J.]]
[[Category: Sygusch, J.]]
[[Category: Tetreault, S.]]
[[Category: Tetreault, S.]]
[[Category: classii fructose 1,6-bisphosphate aldolase]]
[[Category: Classii fructose 1,6-bisphosphate aldolase]]
[[Category: glycolysis]]
[[Category: Glycolysis]]
[[Category: lyase]]
[[Category: Lyase]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:45:42 2008''

Revision as of 14:05, 2 May 2008

File:1dos.gif

Template:STRUCTURE 1dos

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE


OverviewOverview

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.

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 Fri May 2 14:05:39 2008

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