1yfe
From Proteopedia
(New page: 200px<br /><applet load="1yfe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yfe, resolution 2.19Å" /> '''Crystal structure of...) |
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| - | [[Image:1yfe.gif|left|200px]]<br /><applet load="1yfe" size=" | + | [[Image:1yfe.gif|left|200px]]<br /><applet load="1yfe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yfe, resolution 2.19Å" /> | caption="1yfe, resolution 2.19Å" /> | ||
'''Crystal structure of apo fumarase C from Escherichia coli'''<br /> | '''Crystal structure of apo fumarase C from Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Previous crystal structures of fumarase C from Escherichia coli have noted | + | Previous crystal structures of fumarase C from Escherichia coli have noted two occupied dicarboxylate-binding sites termed the active site and the B site. Here, the first known fumarase C structure is reported in which both sites are unoccupied by bound ligand. This so-called ;free' crystal form shows conservation of the active-site water in a similar orientation to that reported in other fumarase C crystal structures. More importantly, a shift of His129 has been observed at the B site. This new crystallographic information suggests the use of water as a permanent member of the active site and the use of an imidazole-imidazolium conversion to control access at the allosteric B site. |
==About this Structure== | ==About this Structure== | ||
| - | 1YFE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2] Full crystallographic information is available from [http:// | + | 1YFE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YFE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: kreb's cycle]] | [[Category: kreb's cycle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:45 2008'' |
Revision as of 14:04, 21 February 2008
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Crystal structure of apo fumarase C from Escherichia coli
Overview
Previous crystal structures of fumarase C from Escherichia coli have noted two occupied dicarboxylate-binding sites termed the active site and the B site. Here, the first known fumarase C structure is reported in which both sites are unoccupied by bound ligand. This so-called ;free' crystal form shows conservation of the active-site water in a similar orientation to that reported in other fumarase C crystal structures. More importantly, a shift of His129 has been observed at the B site. This new crystallographic information suggests the use of water as a permanent member of the active site and the use of an imidazole-imidazolium conversion to control access at the allosteric B site.
About this Structure
1YFE is a Single protein structure of sequence from Escherichia coli. Active as Fumarate hydratase, with EC number 4.2.1.2 Full crystallographic information is available from OCA.
Reference
Structure of free fumarase C from Escherichia coli., Weaver T, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1395-401. Epub, 2005 Sep 28. PMID:16204892
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