1lzk: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1lzk.gif|left|200px]] | [[Image:1lzk.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1lzk", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
| | {{STRUCTURE_1lzk| PDB=1lzk | SCENE= }} | ||
| | |||
}} | |||
'''BACTERIAL HEROIN ESTERASE COMPLEX WITH TRANSITION STATE ANALOG DIMETHYLARSENIC ACID''' | '''BACTERIAL HEROIN ESTERASE COMPLEX WITH TRANSITION STATE ANALOG DIMETHYLARSENIC ACID''' | ||
| Line 30: | Line 27: | ||
[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
[[Category: Zhu, X.]] | [[Category: Zhu, X.]] | ||
[[Category: | [[Category: Alpha/beta hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:27:14 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 00:27, 3 May 2008
BACTERIAL HEROIN ESTERASE COMPLEX WITH TRANSITION STATE ANALOG DIMETHYLARSENIC ACID
OverviewOverview
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.
About this StructureAbout this Structure
1LZK is a Single protein structure of sequence from Rhodococcus sp.. Full crystallographic information is available from OCA.
ReferenceReference
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 Sat May 3 00:27:14 2008