1dos: Difference between revisions

← Older edit Newer edit →

Revision as of 11:41, 20 March 2008

File:1dos.gif

, resolution 1.67Å

Ligands:

and

Activity:

Fructose-bisphosphate aldolase, with EC number 4.1.2.13

Coordinates:

save as pdb, mmCIF, xml

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 Thu Mar 20 10:41:54 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1dos.gif|left|200px]]<br /><applet load="1dos" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dos.gif|left|200px]]
-caption="1dos, resolution 1.67&Aring;" />
-'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''<br />
+ {{Structure
+|PDB= 1dos |SIZE=350|CAPTION= <scene name='initialview01'>1dos</scene>, resolution 1.67&Aring;
+|SITE=
+|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=NH4:AMMONIUM ION'>NH4</scene>
+|ACTIVITY= [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]
+|GENE=
+}}
+'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''
 ==Overview==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-DOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=NH4:'>NH4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOS OCA].
+DOS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DOS 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8836102 8836102]
+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:[http://www.ncbi.nlm.nih.gov/pubmed/8836102 8836102]
 [[Category: Escherichia coli]]
 [[Category: Fructose-bisphosphate aldolase]]
@@ Line 25: / Line 34: @@
 [[Category: lyase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:41:54 2008''