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1gyn

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{{STRUCTURE_1gyn| PDB=1gyn | SCENE= }}
{{STRUCTURE_1gyn| PDB=1gyn | SCENE= }}
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'''CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE'''
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===CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12595741 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12595741}}
==About this Structure==
==About this Structure==
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[[Category: Cadmium]]
[[Category: Cadmium]]
[[Category: Lyase]]
[[Category: Lyase]]
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Revision as of 03:19, 1 July 2008

Template:STRUCTURE 1gyn

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

Template:ABSTRACT PUBMED 12595741

About this Structure

1GYN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from 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:12595741

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