1um0: Difference between revisions
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|PDB= 1um0 |SIZE=350|CAPTION= <scene name='initialview01'>1um0</scene>, resolution 1.95Å | |PDB= 1um0 |SIZE=350|CAPTION= <scene name='initialview01'>1um0</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene> | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | ||
|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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= AROC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori]) | |GENE= AROC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1um0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1um0 OCA], [http://www.ebi.ac.uk/pdbsum/1um0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1um0 RCSB]</span> | |||
}} | }} | ||
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[[Category: Suh, S W.]] | [[Category: Suh, S W.]] | ||
[[Category: Yoon, H J.]] | [[Category: Yoon, H J.]] | ||
[[Category: beta-alpha-beta sandwich fold]] | [[Category: beta-alpha-beta sandwich fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:12:09 2008'' | ||
Revision as of 00:12, 31 March 2008
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| , resolution 1.95Å | |||||||
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| Ligands: | |||||||
| Gene: | AROC (Helicobacter pylori) | ||||||
| Activity: | Chorismate synthase, with EC number 4.2.3.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of chorismate synthase complexed with FMN
OverviewOverview
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 StructureAbout this Structure
1UM0 is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
ReferenceReference
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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