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1fdw
From Proteopedia
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|SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | ||
|LIGAND= <scene name='pdbligand=EST:ESTRADIOL'>EST</scene> | |LIGAND= <scene name='pdbligand=EST:ESTRADIOL'>EST</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Estradiol_17-beta-dehydrogenase Estradiol 17-beta-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.62 1.1.1.62] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Estradiol_17-beta-dehydrogenase Estradiol 17-beta-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.62 1.1.1.62] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdw OCA], [http://www.ebi.ac.uk/pdbsum/1fdw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fdw RCSB]</span> | ||
}} | }} | ||
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[[Category: Housset, D.]] | [[Category: Housset, D.]] | ||
[[Category: Mazza, C.]] | [[Category: Mazza, C.]] | ||
| - | [[Category: EST]] | ||
[[Category: 17-beta-hydroxysteroid]] | [[Category: 17-beta-hydroxysteroid]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
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[[Category: nadp]] | [[Category: nadp]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:21:00 2008'' |
Revision as of 17:21, 30 March 2008
| |||||||
| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Estradiol 17-beta-dehydrogenase, with EC number 1.1.1.62 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 MUTANT H221Q COMPLEXED WITH ESTRADIOL
Overview
Type 1 17beta-hydroxysteroid dehydrogenase (17beta-HSD1), a member of the short chain dehydrogenase reductase (SDR) family, is responsible for the synthesis of 17beta-estradiol, the biologically active estrogen involved in the genesis and development of human breast cancers. Here, we report the crystal structures of the H221L 17beta-HSD1 mutant complexed to NADP+ and estradiol and the H221L mutant/NAD+ and a H221Q mutant/estradiol complexes. These structures provide a complete picture of the NADP+-enzyme interactions involving the flexible 191-199 loop (well ordered in the H221L mutant) and suggest that the hydrophobic residues Phe192-Met193 could facilitate hydride transfer. 17beta-HSD1 appears to be unique among the members of the SDR protein family in that one of the two basic residues involved in the charge compensation of the 2'-phosphate does not belong to the Rossmann-fold motif. The remarkable stabilization of the NADP+ 2'-phosphate by the enzyme also clearly establishes its preference for this cofactor relative to NAD+. Analysis of the catalytic properties of, and estradiol binding to, the two mutants suggests that the His221-steroid O3 hydrogen bond plays an important role in substrate specificity.
About this Structure
1FDW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase., Mazza C, Breton R, Housset D, Fontecilla-Camps JC, J Biol Chem. 1998 Apr 3;273(14):8145-52. PMID:9525918
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