1dos: Difference between revisions
New page: left|200px<br /><applet load="1dos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dos, resolution 1.67Å" /> '''STRUCTURE OF FRUCTOS... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1dos.gif|left|200px]]<br /><applet load="1dos" size=" | [[Image:1dos.gif|left|200px]]<br /><applet load="1dos" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1dos, resolution 1.67Å" /> | caption="1dos, resolution 1.67Å" /> | ||
'''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''<br /> | '''STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE'''<br /> | ||
==Overview== | ==Overview== | ||
The molecular architecture of the Class II E. coli fructose | 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 Structure== | ==About this Structure== | ||
1DOS 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 ZN and NH4 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:// | 1DOS 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]. | ||
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[Category: lyase]] | [[Category: lyase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:49 2008'' | ||
Revision as of 13:18, 21 February 2008
|
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 with and as ligands. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 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 Feb 21 12:18:49 2008