1gyn
From Proteopedia
(New page: 200px<br /><applet load="1gyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gyn, resolution 2.00Å" /> '''CLASS II FRUCTOSE 1,...) |
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| - | [[Image:1gyn.jpg|left|200px]]<br /><applet load="1gyn" size=" | + | [[Image:1gyn.jpg|left|200px]]<br /><applet load="1gyn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gyn, resolution 2.00Å" /> | caption="1gyn, resolution 2.00Å" /> | ||
'''CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE'''<br /> | '''CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE'''<br /> | ||
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| + | ==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== | ==About this Structure== | ||
| - | 1GYN 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 CD as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1GYN 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=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1GYN OCA]. |
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| + | ==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12595741 12595741] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Fructose-bisphosphate aldolase]] | [[Category: Fructose-bisphosphate aldolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Berry, A.]] | [[Category: Berry, A.]] | ||
| - | [[Category: Hall, D | + | [[Category: Hall, D R.]] |
| - | [[Category: Hunter, W | + | [[Category: Hunter, W N.]] |
| - | [[Category: Kemp, L | + | [[Category: Kemp, L E.]] |
| - | [[Category: Leonard, G | + | [[Category: Leonard, G A.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:55:29 2008'' |
Revision as of 10:55, 21 February 2008
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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 Escherichia coli with as ligand. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 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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