1qz3
From Proteopedia
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|PDB= 1qz3 |SIZE=350|CAPTION= <scene name='initialview01'>1qz3</scene>, resolution 2.30Å | |PDB= 1qz3 |SIZE=350|CAPTION= <scene name='initialview01'>1qz3</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HDS:1-HEXADECANOSULFONIC ACID'>HDS</scene> | + | |LIGAND= <scene name='pdbligand=HDS:1-HEXADECANOSULFONIC+ACID'>HDS</scene>, <scene name='pdbligand=X:2'-DEOXY-N7-(8,9-DIHYDRO-9-HYDROXY-10-DEHYDROXY-AFLATOXIN)GUANOSINE+MONOPHOSPHATE'>X</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1evq|1evq]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qz3 OCA], [http://www.ebi.ac.uk/pdbsum/1qz3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qz3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Rossi, M.]] | [[Category: Rossi, M.]] | ||
[[Category: Simone, G De.]] | [[Category: Simone, G De.]] | ||
| - | [[Category: HDS]] | ||
[[Category: alpha/beta hydrolase fold]] | [[Category: alpha/beta hydrolase fold]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:59 2008'' |
Revision as of 20:21, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Carboxylesterase, with EC number 3.1.1.1 | ||||||
| Related: | 1evq
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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