Sandbox Reserved 987

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<scene name='69/691529/Cocaine_esterase/1'>Cocaine Esterase</scene>
<scene name='69/691529/Cocaine_esterase/1'>Cocaine Esterase</scene>
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Cocaine Esterase is a globular protein that is expressed in the cytosol of ''Rhodococcus'' strain of bacteria, containing 574 residues divided into three domains. Domain I is a α/β hydrolase fold-containing domain consisting of residues 1-144 and residues 241-354 with the active site His-287. Domain II is a α-helical consisting of residues 145-240, making up seven helices inserted between β6 and β7 of Domain I. Helices two through six together form a five helix core with helices two and three combine to make a lid-like structure over the active site, His-287. Domain III is made up of residues 355-574 with mostly β-structure and a β-barrel-like core connected by 6 cross over loops, forming a jelly roll-like topology.
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Cocaine Esterase is a globular protein that is expressed in the cytosol of ''Rhodococcus'' strain of bacteria, containing 574 residues divided into three domains. Domain I is a α/β hydrolase fold-containing domain consisting of residues 1-144 and residues 241-354 with the active site His-287. Domain II is a α-helical consisting of residues 145-240, making up seven helices inserted between β6 and β7 of Domain I. Helices two through six together form a five helix core with helices two and three combine to make a lid-like structure over the active site, His-287. Domain III is made up of residues 355-574 with mostly β-structure and a β-barrel-like core connected by 6 cross over loops, forming a jelly roll-like topology.<sup><ref>Narasimhan, D.; Woods, J.H.; Sunahara, R.K. “Bacterial cocaine esterase: a protein-based therapy for cocaine overdose and addiction.” ''Future Med Chem.'' 2012, 4, 2: 137-150.</ref></sup>
== Function ==
== Function ==

Revision as of 00:47, 25 February 2015

This Sandbox is Reserved from 20/01/2015, through 30/04/2016 for use in the course "CHM 463" taught by Mary Karpen at the Grand Valley State University. This reservation includes Sandbox Reserved 987 through Sandbox Reserved 996.
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Contents

Cocaine Esterase

Cocaine Esterase

Drag the structure with the mouse to rotate

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.

Background

Cocaine Esterase (CocE) is the most efficient protein to hydrolyze the cocaine domain known to date in vivo.[3] Cocaine Esterase is used in bacterium Rhodococcus which hydrolyzes the cocaine that it uptakes and uses it for carbons and nitrogens. Although this protein metabolizes cocaine in bacterium, it is sure to induce an immune response as it is foreign to the human body. This could mitigate the effects of CocE if a person had suffered from cocaine toxicity.

Structure

Cocaine Esterase is a globular protein that is expressed in the cytosol of Rhodococcus strain of bacteria, containing 574 residues divided into three domains. Domain I is a α/β hydrolase fold-containing domain consisting of residues 1-144 and residues 241-354 with the active site His-287. Domain II is a α-helical consisting of residues 145-240, making up seven helices inserted between β6 and β7 of Domain I. Helices two through six together form a five helix core with helices two and three combine to make a lid-like structure over the active site, His-287. Domain III is made up of residues 355-574 with mostly β-structure and a β-barrel-like core connected by 6 cross over loops, forming a jelly roll-like topology.[4]

Function

Cocaine esterase is used to catalyze the following reaction: cocaine + H2O ←→ ecgonine methyl ester + benzoate [5] Reaction mechanism for cocaine esterase-catalyzed hydrolyses of (+)- and (-)-cocaine: unexpected common rate-determining step. Liu J1, Zhao X, Yang W, Zhan CG.

Medical Relevance

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.


References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
  3. ↑ "Effects of cocaine esterase following its repeated administration with cocaine in mice" Mei-Chaun Ko, Diwahar Narasimhan, Aaron A. Berlin, Nicholas W. Lukacs, Roger K. Sunahara, James H. Woods. Drug and Alcohol Dependence 1 May 2009;101:202-09. doi: 10.1016/j.drugalcdep.2009.01.002
  4. ↑ Narasimhan, D.; Woods, J.H.; Sunahara, R.K. “Bacterial cocaine esterase: a protein-based therapy for cocaine overdose and addiction.” Future Med Chem. 2012, 4, 2: 137-150.
  5. ↑ Cocaine esterase From Wikipedia, the free encyclopedia
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