This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1lzl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lzl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lzl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lzl| PDB=1lzl | SCENE= }}
{{STRUCTURE_1lzl| PDB=1lzl | SCENE= }}
-
'''Bacterial Heroin Esterase'''
+
===Bacterial Heroin Esterase===
-
==Overview==
+
<!--
-
The crystal structures of an acetyl esterase, HerE, and its complex with an inhibitor dimethylarsinic acid have been determined at 1.30- and 1.45-A resolution, respectively. Although the natural substrate for the enzyme is unknown, HerE hydrolyzes the acetyl groups from heroin to yield morphine and from phenyl acetate to yield phenol. Recently, the activity of the enzyme toward heroin has been exploited to develop a heroin biosensor, which affords higher sensitivity than other currently available detection methods. The crystal structure reveals a single domain with the canonical alpha/beta hydrolase fold with an acyl binding pocket that snugly accommodates the acetyl substituent of the substrate and three backbone amides that form a tripartite oxyanion hole. In addition, a covalent adduct was observed between the active site serine and dimethylarsinic acid, which inhibits the enzyme. This crystal structure provides the first example of an As-containing compound in a serine esterase active site and the first example of covalent modification of serine by arsenic. Thus, the HerE complex reveals the structural basis for the broad scope inhibition of serine hydrolases by As(V)-containing organic compounds.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12421810}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12421810 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12421810}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Zhu, X.]]
[[Category: Zhu, X.]]
[[Category: Alpha/beta hydrolase]]
[[Category: Alpha/beta hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:27:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:53:16 2008''

Revision as of 19:53, 2 July 2008

Image:1lzl.png

Template:STRUCTURE 1lzl

Bacterial Heroin Esterase

Template:ABSTRACT PUBMED 12421810

About this Structure

1LZL is a Single protein structure of sequence from Rhodococcus sp.. Full crystallographic information is available from OCA.

Reference

Observation of an arsenic adduct in an acetyl esterase crystal structure., Zhu X, Larsen NA, Basran A, Bruce NC, Wilson IA, J Biol Chem. 2003 Jan 17;278(3):2008-14. Epub 2002 Nov 5. PMID:12421810

Page seeded by OCA on Wed Jul 2 22:53:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lzl"
Personal tools