1GYN

Class II fructose 1,6-bisphosphate aldolase with Cadmium (not Zinc) in the active site

Summary for 1GYN

• Entry DOI: 10.2210/pdb1gyn/pdb
• Related: 1B57 1DOS 1ZEN
• Descriptor: FRUCTOSE-BISPHOSPHATE ALDOLASE II, CADMIUM ION (3 entities in total)
• Functional Keywords: lyase, cadmium, aldolase
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 39622.01

Authors

Hall, D.R.,Kemp, L.E.,Leonard, G.A.,Berry, A.,Hunter, W.N. (deposition date: 2002-04-27, release date: 2003-02-26, Last modification date: 2023-12-13)

Primary citation

Hall, D.R.,Kemp, L.E.,Leonard, G.A.,Marshall, K.,Berry, A.,Hunter, W.N.
The Organization of Divalent Cations in the Active Site of Cadmium Escherichia Coli Fructose 1,6-Bisphosphate Aldolase
Acta Crystallogr.,Sect.D, 59:611-, 2003

PubMed Abstract: 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.

PubMed: 12595741
DOI: 10.1107/S0907444902023661

Experimental method

X-RAY DIFFRACTION (2 Å)