2ahc
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= ubiC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ubiC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1tt8|1tt8]], [[1xlr|1xlr]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ahc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahc OCA], [http://www.ebi.ac.uk/pdbsum/2ahc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ahc RCSB]</span> | ||
}} | }} | ||
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[[Category: Gallagher, D T.]] | [[Category: Gallagher, D T.]] | ||
[[Category: Smith, N N.]] | [[Category: Smith, N N.]] | ||
| - | [[Category: VNL]] | ||
[[Category: 123654 antiparallel sheet]] | [[Category: 123654 antiparallel sheet]] | ||
[[Category: internal active site]] | [[Category: internal active site]] | ||
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[[Category: unique fold]] | [[Category: unique 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 01:52:40 2008'' |
Revision as of 22:52, 30 March 2008
| |||||||
| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ubiC (Escherichia coli) | ||||||
| Related: | 1tt8, 1xlr
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Chorismate lyase with inhibitor Vanilate
Overview
Chorismate lyase (CL) removes the pyruvyl group from chorismate to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. We previously reported the crystal structure at 1.4A resolution of the Escherichia coli CL with bound 4HB product, showing that the product is bound in an internal cavity behind two flaps. To provide a more complete basis for understanding CL's unusual ligand-binding properties and mechanism of action, we now report four crystal structures of CL mutants and inhibitor complexes, together with binding and activity measurements and molecular dynamics simulations. First, an ultrahigh resolution (1.0A) crystal structure of the CL*product complex reveals details of a substrate-sized internal cavity, also behind the flaps, near the product site. Second, a 2.4A structure of CL complexed with the inhibitor vanillate shows the flaps partly opened relative to their product-bound positions. Third, a 2.0A structure of the G90A mutant with bound product reveals the basis for tighter product binding and kinetic effects of this active site mutation. Fourth, the combination of the G90A mutation with the vanillate inhibitor produces a 1.9A structure containing two inhibitor molecules, one in the product site and the other in the adjacent cavity. The two sites are connected by a short tunnel that is partly open at each end, suggesting that CL may operate via a 2-site or tunnel mechanism.
About this Structure
2AHC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural analysis of ligand binding and catalysis in chorismate lyase., Smith N, Roitberg AE, Rivera E, Howard A, Holden MJ, Mayhew M, Kaistha S, Gallagher DT, Arch Biochem Biophys. 2006 Jan 1;445(1):72-80. Epub 2005 Nov 22. PMID:16343413
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