2h7c

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2h7c.gif|left|200px]]<br /><applet load="2h7c" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2h7c.gif|left|200px]]
-
caption="2h7c, resolution 2.00&Aring;" />
+
 
-
'''Crystal structure of human carboxylesterase in complex with Coenzyme A'''<br />
+
{{Structure
 +
|PDB= 2h7c |SIZE=350|CAPTION= <scene name='initialview01'>2h7c</scene>, resolution 2.00&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=COA:COENZYME A'>COA</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]
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of human carboxylesterase in complex with Coenzyme A'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
2H7C 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=NDG:'>NDG</scene>, <scene name='pdbligand=SIA:'>SIA</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=COA:'>COA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7C OCA].
+
2H7C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7C OCA].
==Reference==
==Reference==
-
Multisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1., Bencharit S, Edwards CC, Morton CL, Howard-Williams EL, Kuhn P, Potter PM, Redinbo MR, J Mol Biol. 2006 Oct 13;363(1):201-14. Epub 2006 Aug 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16962139 16962139]
+
Multisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1., Bencharit S, Edwards CC, Morton CL, Howard-Williams EL, Kuhn P, Potter PM, Redinbo MR, J Mol Biol. 2006 Oct 13;363(1):201-14. Epub 2006 Aug 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16962139 16962139]
[[Category: Carboxylesterase]]
[[Category: Carboxylesterase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 33: Line 42:
[[Category: hydrolase]]
[[Category: hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:38:55 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:13:36 2008''

Revision as of 15:13, 20 March 2008

Image:2h7c.gif


PDB ID 2h7c

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , , , and
Activity: Carboxylesterase, with EC number 3.1.1.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human carboxylesterase in complex with Coenzyme A


Contents

Overview

Human carboxylesterase 1 (hCE1) is a drug and endobiotic-processing serine hydrolase that exhibits relatively broad substrate specificity. It has been implicated in a variety of endogenous cholesterol metabolism pathways including the following apparently disparate reactions: cholesterol ester hydrolysis (CEH), fatty acyl Coenzyme A hydrolysis (FACoAH), acyl-Coenzyme A:cholesterol acyltransfer (ACAT), and fatty acyl ethyl ester synthesis (FAEES). The structural basis for the ability of hCE1 to perform these catalytic actions involving large substrates and products has remained unclear. Here we present four crystal structures of the hCE1 glycoprotein in complexes with the following endogenous substrates or substrate analogues: Coenzyme A, the fatty acid palmitate, and the bile acids cholate and taurocholate. While the active site of hCE1 was known to be promiscuous and capable of interacting with a variety of chemically distinct ligands, these structures reveal that the enzyme contains two additional ligand-binding sites and that each site also exhibits relatively non-specific ligand-binding properties. Using this multisite promiscuity, hCE1 appears structurally capable of assembling several catalytic events depending, apparently, on the physiological state of the cellular environment. These results expand our understanding of enzyme promiscuity and indicate that, in the case of hCE1, multiple non-specific sites are employed to perform distinct catalytic actions.

Disease

Known disease associated with this structure: Monocyte carboxylesterase deficiency (1) OMIM:[114835]

About this Structure

2H7C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Multisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1., Bencharit S, Edwards CC, Morton CL, Howard-Williams EL, Kuhn P, Potter PM, Redinbo MR, J Mol Biol. 2006 Oct 13;363(1):201-14. Epub 2006 Aug 15. PMID:16962139

Page seeded by OCA on Thu Mar 20 17:13:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h7c"
Personal tools