1umf
From Proteopedia
(New page: 200px<br /><applet load="1umf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1umf, resolution 2.25Å" /> '''crystal structure of...) |
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| - | [[Image:1umf.gif|left|200px]]<br /><applet load="1umf" size=" | + | [[Image:1umf.gif|left|200px]]<br /><applet load="1umf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1umf, resolution 2.25Å" /> | caption="1umf, resolution 2.25Å" /> | ||
'''crystal structure of chorismate synthase'''<br /> | '''crystal structure of chorismate synthase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Chorismate synthase catalyzes the conversion of 5-enolpyruvylshikimate | + | Chorismate synthase catalyzes the conversion of 5-enolpyruvylshikimate 3-phosphate to chorismate in the shikimate pathway, which represents an attractive target for discovering antimicrobial agents and herbicides. Chorismate serves as a common precursor for the synthesis of aromatic amino acids and many aromatic compounds in microorganisms and plants. Chorismate synthase requires reduced FMN as a cofactor but the catalyzed reaction involves no net redox change. Here, we have determined the crystal structure of chorismate synthase from Helicobacter pylori in both FMN-bound and FMN-free forms. It is a tetrameric enzyme, with each monomer possessing a novel "beta-alpha-beta sandwich fold". Highly conserved regions, including several flexible loops, cluster together around the bound FMN to form the active site. The unique FMN-binding site is formed largely by a single subunit, with a small contribution from a neighboring subunit. The isoalloxazine ring of the bound FMN is significantly non-planar. Our structure illuminates the essential functional roles played by the cofactor. |
==About this Structure== | ==About this Structure== | ||
| - | 1UMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Active as [http://en.wikipedia.org/wiki/Chorismate_synthase Chorismate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.5 4.2.3.5] Full crystallographic information is available from [http:// | + | 1UMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Active as [http://en.wikipedia.org/wiki/Chorismate_synthase Chorismate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.5 4.2.3.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ahn, H | + | [[Category: Ahn, H J.]] |
[[Category: Lee, B.]] | [[Category: Lee, B.]] | ||
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
| - | [[Category: Yoon, H | + | [[Category: Yoon, H J.]] |
[[Category: beta-alpha-beta sandwich fold]] | [[Category: beta-alpha-beta sandwich fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:13 2008'' |
Revision as of 13:26, 21 February 2008
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crystal structure of chorismate synthase
Overview
Chorismate synthase catalyzes the conversion of 5-enolpyruvylshikimate 3-phosphate to chorismate in the shikimate pathway, which represents an attractive target for discovering antimicrobial agents and herbicides. Chorismate serves as a common precursor for the synthesis of aromatic amino acids and many aromatic compounds in microorganisms and plants. Chorismate synthase requires reduced FMN as a cofactor but the catalyzed reaction involves no net redox change. Here, we have determined the crystal structure of chorismate synthase from Helicobacter pylori in both FMN-bound and FMN-free forms. It is a tetrameric enzyme, with each monomer possessing a novel "beta-alpha-beta sandwich fold". Highly conserved regions, including several flexible loops, cluster together around the bound FMN to form the active site. The unique FMN-binding site is formed largely by a single subunit, with a small contribution from a neighboring subunit. The isoalloxazine ring of the bound FMN is significantly non-planar. Our structure illuminates the essential functional roles played by the cofactor.
About this Structure
1UMF is a Single protein structure of sequence from Helicobacter pylori. Active as Chorismate synthase, with EC number 4.2.3.5 Full crystallographic information is available from OCA.
Reference
Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights., Ahn HJ, Yoon HJ, Lee B 2nd, Suh SW, J Mol Biol. 2004 Feb 27;336(4):903-15. PMID:15095868
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