1um0
From Proteopedia
(New page: 200px<br /><applet load="1um0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1um0, resolution 1.95Å" /> '''Crystal structure of...) |
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| - | [[Image:1um0.jpg|left|200px]]<br /><applet load="1um0" size=" | + | [[Image:1um0.jpg|left|200px]]<br /><applet load="1um0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1um0, resolution 1.95Å" /> | caption="1um0, resolution 1.95Å" /> | ||
'''Crystal structure of chorismate synthase complexed with FMN'''<br /> | '''Crystal structure of chorismate synthase complexed with FMN'''<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== | ||
| - | 1UM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1UM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1UM0 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: FMN]] | [[Category: FMN]] | ||
[[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 15:26:01 2008'' |
Revision as of 13:26, 21 February 2008
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Crystal structure of chorismate synthase complexed with FMN
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
1UM0 is a Single protein structure of sequence from Helicobacter pylori with as ligand. 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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