1gyn: Difference between revisions
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'''CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE''' | '''CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE''' | ||
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[[Category: Kemp, L E.]] | [[Category: Kemp, L E.]] | ||
[[Category: Leonard, G A.]] | [[Category: Leonard, G A.]] | ||
[[Category: | [[Category: Aldolase]] | ||
[[Category: | [[Category: Cadmium]] | ||
[[Category: | [[Category: Lyase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:11:12 2008'' | |||
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Revision as of 18:11, 2 May 2008
CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE
OverviewOverview
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 StructureAbout this Structure
1GYN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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:12595741 Page seeded by OCA on Fri May 2 18:11:12 2008