View source for 1gyn

[[Image:1gyn.jpg|left|200px]]

 {{Structure
|PDB= 1gyn |SIZE=350|CAPTION= <scene name='initialview01'>1gyn</scene>, resolution 2.00&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>
|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>
|GENE= 
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyn OCA], [http://www.ebi.ac.uk/pdbsum/1gyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gyn RCSB]</span>
}}

'''CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE'''


==Overview==
Previously determined crystal structures of the zinc enzyme Escherichia coli class II fructose-1,6-bisphosphate aldolase display good agreement for the protein structure but a differing metal-ion organization in the active site. The structure of the enzyme with Cd(2+) in place of Zn(2+) has now been determined to 2.0 A resolution to facilitate cation identification. The protein structure was essentially identical to other structures and five Cd(2+) positions were identified. Two of the cations are at the active site; one corresponds to the catalytic ion and the other provides a structural contribution. These Cd(2+) sites are equivalent to two Zn(2+) ions observed when the enzyme is complexed with a transition-state mimic and confirm our assignment of the roles played by these ions.

==About this Structure==
1GYN 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=1GYN OCA]. 

==Reference==
The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase., Hall DR, Kemp LE, Leonard GA, Marshall K, Berry A, Hunter WN, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):611-4. Epub 2003, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595741 12595741]
[[Category: Escherichia coli]]
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Single protein]]
[[Category: Berry, A.]]
[[Category: Hall, D R.]]
[[Category: Hunter, W N.]]
[[Category: Kemp, L E.]]
[[Category: Leonard, G A.]]
[[Category: aldolase]]
[[Category: cadmium]]
[[Category: lyase]]

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