1fjh: Difference between revisions

Revision as of 03:21, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fjh.png

Template:STRUCTURE 1fjh

THE CRYSTAL STRUCTURE OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILYTHE CRYSTAL STRUCTURE OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY

Template:ABSTRACT PUBMED 11007791

About this StructureAbout this Structure

1FJH is a Single protein structure of sequence from Comamonas testosteroni. Full crystallographic information is available from OCA.

ReferenceReference

The crystal structure of 3alpha -hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family., Grimm C, Maser E, Mobus E, Klebe G, Reuter K, Ficner R, J Biol Chem. 2000 Dec 29;275(52):41333-9. PMID:11007791

Page seeded by OCA on Tue Jul 1 03:21:47 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fjh.jpg|left|200px]]
+{{Seed}}
+[[Image:1fjh.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1fjh|  PDB=1fjh  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY'''
+===THE CRYSTAL STRUCTURE OF 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE FROM COMAMONAS TESTOSTERONI, A MEMBER OF THE SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY===
-==Overview==
+<!--
-The crystal structure of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni (3alpha-HSDH) as well as the structure of its binary complex with NAD(+) have been solved at 1.68-A and 1.95-A resolution, respectively. The enzyme is a member of the short chain dehydrogenase/reductase (SDR) family. Accordingly, the active center and the conformation of the bound nucleotide cofactor closely resemble those of other SDRs. The crystal structure reveals one homodimer per asymmetric unit representing the physiologically active unity. Dimerization takes place via an interface essentially built-up by helix alphaG and strand betaG of each subunit. So far this type of intermolecular contact has exclusively been observed in homotetrameric SDRs but never in the structure of a homodimeric SDR. The formation of a tetramer is blocked in 3alpha-HSDH by the presence of a predominantly alpha-helical subdomain which is missing in all other SDRs of known structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_11007791}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11007791 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11007791}}
 ==About this Structure==
@@ Line 36: / Line 40: @@
 [[Category: Steroid]]
 [[Category: Xenobiotic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:24:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:21:47 2008''