1p0m
From Proteopedia
(New page: 200px<br /> <applet load="1p0m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p0m, resolution 2.38Å" /> '''Crystal structure o...) |
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| - | [[Image:1p0m.gif|left|200px]]<br /> | + | [[Image:1p0m.gif|left|200px]]<br /><applet load="1p0m" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1p0m" size=" | + | |
caption="1p0m, resolution 2.38Å" /> | caption="1p0m, resolution 2.38Å" /> | ||
'''Crystal structure of human butyryl cholinesterase in complex with a choline molecule'''<br /> | '''Crystal structure of human butyryl cholinesterase in complex with a choline molecule'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cholinesterases are among the most efficient enzymes known. They are | + | Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave. Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents. Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding. As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase. The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected. An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1P0M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, SO4, CL, MES, CHT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cholinesterase Cholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.8 3.1.1.8] Full crystallographic information is available from [http:// | + | 1P0M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=MES:'>MES</scene>, <scene name='pdbligand=CHT:'>CHT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cholinesterase Cholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.8 3.1.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fontecilla-Camps, J | + | [[Category: Fontecilla-Camps, J C.]] |
[[Category: Lockridge, O.]] | [[Category: Lockridge, O.]] | ||
[[Category: Masson, P.]] | [[Category: Masson, P.]] | ||
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[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:43 2008'' |
Revision as of 12:23, 21 February 2008
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Crystal structure of human butyryl cholinesterase in complex with a choline molecule
Contents |
Overview
Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave. Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents. Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding. As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase. The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected. An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
Disease
Known diseases associated with this structure: Apnea, postanesthetic OMIM:[177400]
About this Structure
1P0M is a Single protein structure of sequence from Homo sapiens with , , , , and as ligands. Active as Cholinesterase, with EC number 3.1.1.8 Full crystallographic information is available from OCA.
Reference
Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products., Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F, J Biol Chem. 2003 Oct 17;278(42):41141-7. Epub 2003 Jul 17. PMID:12869558
Page seeded by OCA on Thu Feb 21 14:23:43 2008
Categories: Cholinesterase | Homo sapiens | Single protein | Fontecilla-Camps, J C. | Lockridge, O. | Masson, P. | Nachon, F. | Nicolet, Y. | CHT | CL | GOL | MES | NAG | SO4 | Choline | Serine hydrolase
