1ov4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ov4.jpg|left|200px]]<br /><applet load="1ov4" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ov4.jpg|left|200px]]
-
caption="1ov4, resolution 2.7&Aring;" />
+
 
-
'''Crystal structure of human DHEA-ST complexed with androsterone'''<br />
+
{{Structure
 +
|PDB= 1ov4 |SIZE=350|CAPTION= <scene name='initialview01'>1ov4</scene>, resolution 2.7&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=AE2:AETIOCHOLANOLONE'>AE2</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Alcohol_sulfotransferase Alcohol sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.2 2.8.2.2]
 +
|GENE= SULT2A1 OR STD OR HST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''Crystal structure of human DHEA-ST complexed with androsterone'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
1OV4 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=SO4:'>SO4</scene> and <scene name='pdbligand=AE2:'>AE2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_sulfotransferase Alcohol sulfotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.2.2 2.8.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OV4 OCA].
+
1OV4 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=1OV4 OCA].
==Reference==
==Reference==
-
Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex., Chang HJ, Shi R, Rehse P, Lin SX, J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14573603 14573603]
+
Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex., Chang HJ, Shi R, Rehse P, Lin SX, J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14573603 14573603]
[[Category: Alcohol sulfotransferase]]
[[Category: Alcohol sulfotransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 25: Line 34:
[[Category: alpha/beta fold]]
[[Category: alpha/beta fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:52 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:59 2008''

Revision as of 11:16, 20 March 2008


PDB ID 1ov4

Drag the structure with the mouse to rotate
, resolution 2.7Å
Ligands: and
Gene: SULT2A1 OR STD OR HST (Homo sapiens)
Activity: Alcohol sulfotransferase, with EC number 2.8.2.2
Coordinates: save as pdb, mmCIF, xml



Crystal structure of human DHEA-ST complexed with androsterone


Contents

Overview

In steroid biosynthesis, human dehydroepiandrosterone sulfotransferase (DHEA-ST) in the adrenals has been reported to catalyze the transfer of the sulfonate group from 3'-phosphoadenosine-5'-phosphosulfate to dehydroepiandrosterone (DHEA). DHEA and its sulfate play roles as steroid precursors; however, the role of the enzyme in the catabolism of androgens is poorly understood. Androsterone sulfate is clinically recognized as one of the major androgen metabolites found in urine. Here it is demonstrated that this enzyme recognizes androsterone (ADT) as a cognate substrate with similar kinetics but a 2-fold specificity and stronger substrate inhibition than DHEA. The structure of human DHEA-ST in complex with ADT has been solved at 2.7 A resolution, confirming ADT recognition. Structural analysis has revealed the binding mode of ADT differs from that of DHEA, despite the similarity of the overall structure between the ADT and the DHEA binary complexes. Our results identify that this human enzyme is an ADT sulfotransferase as well as a DHEA sulfotransferase, implying an important role in steroid homeostasis for the adrenals and liver.

Disease

Known diseases associated with this structure: Histidinemia OMIM:[609457], Selective T-cell defect OMIM:[176947]

About this Structure

1OV4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex., Chang HJ, Shi R, Rehse P, Lin SX, J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. PMID:14573603

Page seeded by OCA on Thu Mar 20 13:15:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools