2cht
From Proteopedia
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| - | [[Image:2cht.gif|left|200px]] | + | [[Image:2cht.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG''' | + | {{Structure |
| + | |PDB= 2cht |SIZE=350|CAPTION= <scene name='initialview01'>2cht</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID'>TSA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CHT is a [ | + | 2CHT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CHT OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog., Chook YM, Ke H, Lipscomb WN, Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8600-3. PMID:[http:// | + | Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog., Chook YM, Ke H, Lipscomb WN, Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8600-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8378335 8378335] |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Chorismate mutase]] | [[Category: Chorismate mutase]] | ||
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[[Category: isomerase]] | [[Category: isomerase]] | ||
| - | ''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 16:15:34 2008'' |
Revision as of 14:15, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | |||||||
| Activity: | Chorismate mutase, with EC number 5.4.99.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURES OF THE MONOFUNCTIONAL CHORISMATE MUTASE FROM BACILLUS SUBTILIS AND ITS COMPLEX WITH A TRANSITION STATE ANALOG
Overview
We have solved the structure of a chorismate mutase (chorismate pyruvatemutase, EC 5.4.99.5), the 1.9-A crystal structure of the monofunctional enzyme from Bacillus subtilis. The structure determination process was an unusual one, involving 12 monomers of the enzyme in the asymmetric unit. This structure was solved by the multiple isomorphous replacement method with partial structure phase combination and molecular averaging. The final model, which includes 1380 residues and 522 water molecules in an asymmetric unit, has been refined at 1.9 A and the current crystallographic R value is 0.201. The B. subtilis chorismate mutase is a homotrimer, with beta-sheets from each monomer packing to form the core of a pseudo-alpha beta-barrel with helices on the outside of the trimer. In addition, the active sites have been located by using data from a complex with an endo-oxabicyclic inhibitor that mimics the transition state of the reaction. The structure of this complex has been refined to 2.2 A with a current R value of 0.182 for a model that includes 1388 residues, 12 inhibitor molecules, and 530 water molecules in the asymmetric unit. In each trimer, three equivalent active sites are located at the interfaces of two adjacent subunits.
About this Structure
2CHT is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog., Chook YM, Ke H, Lipscomb WN, Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8600-3. PMID:8378335
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