1qz3
From Proteopedia
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| - | [[Image:1qz3.gif|left|200px]] | + | [[Image:1qz3.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE''' | + | {{Structure |
| + | |PDB= 1qz3 |SIZE=350|CAPTION= <scene name='initialview01'>1qz3</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HDS:1-HEXADECANOSULFONIC ACID'>HDS</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QZ3 is a [ | + | 1QZ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QZ3 OCA]. |
==Reference== | ==Reference== | ||
| - | A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis., De Simone G, Mandrich L, Menchise V, Giordano V, Febbraio F, Rossi M, Pedone C, Manco G, J Biol Chem. 2004 Feb 20;279(8):6815-23. Epub 2003 Nov 15. PMID:[http:// | + | A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis., De Simone G, Mandrich L, Menchise V, Giordano V, Febbraio F, Rossi M, Pedone C, Manco G, J Biol Chem. 2004 Feb 20;279(8):6815-23. Epub 2003 Nov 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14617621 14617621] |
[[Category: Alicyclobacillus acidocaldarius]] | [[Category: Alicyclobacillus acidocaldarius]] | ||
[[Category: Carboxylesterase]] | [[Category: Carboxylesterase]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 13:44:40 2008'' |
Revision as of 11:44, 20 March 2008
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| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Carboxylesterase, with EC number 3.1.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE
Overview
The reaction mechanism of the esterase 2 (EST2) from Alicyclobacillus acidocaldarius was studied at the kinetic and structural level to shed light on the mechanism of activity and substrate specificity increase previously observed in its double mutant M211S/R215L. In particular, the values of kinetic constants (k1, k(-1), k2, and k3) along with activation energies (E1, E(-1), E2, and E3) were measured for wild type and mutant enzyme. The previously suggested substrate-induced switch in the reaction mechanism from kcat=k3 with a short acyl chain substrate (p-nitrophenyl hexanoate) to kcat=k2 with a long acyl chain substrate (p-nitrophenyl dodecanoate) was validated. The inhibition afforded by an irreversible inhibitor (1-hexadecanesulfonyl chloride), structurally related to p-nitrophenyl dodecanoate, was studied by kinetic analysis. Moreover the three-dimensional structure of the double mutant bound to this inhibitor was determined, providing essential information on the enzyme mechanism. In fact, structural analysis explained the observed substrate-induced switch because of an inversion in the binding mode of the long acyl chain derivatives with respect to the acyl- and alcohol-binding sites.
About this Structure
1QZ3 is a Single protein structure of sequence from Alicyclobacillus acidocaldarius. Full crystallographic information is available from OCA.
Reference
A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis., De Simone G, Mandrich L, Menchise V, Giordano V, Febbraio F, Rossi M, Pedone C, Manco G, J Biol Chem. 2004 Feb 20;279(8):6815-23. Epub 2003 Nov 15. PMID:14617621
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