1umf: Difference between revisions
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'''crystal structure of chorismate synthase''' | {{Structure | ||
|PDB= 1umf |SIZE=350|CAPTION= <scene name='initialview01'>1umf</scene>, resolution 2.25Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''crystal structure of chorismate synthase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1UMF is a [ | 1UMF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMF OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15095868 15095868] | ||
[[Category: Chorismate synthase]] | [[Category: Chorismate synthase]] | ||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
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[[Category: beta-alpha-beta sandwich fold]] | [[Category: beta-alpha-beta sandwich fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:33:53 2008'' | ||
Revision as of 12:34, 20 March 2008
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| 1umf, resolution 2.25Å | |||||||||||||
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| Activity: | Chorismate synthase, with EC number 4.2.3.5 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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