1fdv
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1fdv |SIZE=350|CAPTION= <scene name='initialview01'>1fdv</scene>, resolution 3.1Å | |PDB= 1fdv |SIZE=350|CAPTION= <scene name='initialview01'>1fdv</scene>, resolution 3.1Å | ||
|SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1fdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fdv OCA], [http://www.ebi.ac.uk/pdbsum/1fdv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fdv RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Housset, D.]] | [[Category: Housset, D.]] | ||
[[Category: Mazza, C.]] | [[Category: Mazza, C.]] | ||
| - | [[Category: NAD]] | ||
| - | [[Category: SO4]] | ||
[[Category: 17-beta-hydroxysteroid]] | [[Category: 17-beta-hydroxysteroid]] | ||
[[Category: dehydrogenase]] | [[Category: dehydrogenase]] | ||
| Line 34: | Line 35: | ||
[[Category: nad]] | [[Category: nad]] | ||
| - | ''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 20:21:09 2008'' |
Revision as of 17:21, 30 March 2008
| |||||||
| , resolution 3.1Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 H221L COMPLEXED WITH NAD+
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
1FDV 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
Page seeded by OCA on Sun Mar 30 20:21:09 2008
