scholarly journals The crystal structure of a crustacean prophenoloxidase provides a clue to understanding the functionality of the type 3 copper proteins

FEBS Journal ◽  
2014 ◽  
Vol 281 (11) ◽  
pp. 2659-2673 ◽  
Author(s):  
Taro Masuda ◽  
Kyosuke Momoji ◽  
Takashi Hirata ◽  
Bunzo Mikami
Keyword(s):  
Crystal Structure ◽  
Copper Proteins ◽  
Type 3

The Crystal Structure of Catechol Oxidase:  New Insight into the Function of Type-3 Copper Proteins

2002 ◽  
Vol 35 (3) ◽  
pp. 183-191 ◽  
Author(s):  
Carsten Gerdemann ◽  
Christoph Eicken ◽  
Bernt Krebs
Keyword(s):  
Crystal Structure ◽  
Catechol Oxidase ◽  
Copper Proteins ◽  
Type 3 ◽  
Insight Into

Dicopper complexes of a macrocyclic ligand as models for type 3 copper proteins

1983 ◽  
Vol 105 (17) ◽  
pp. 5693-5695 ◽  
Author(s):  
S. Martin Nelson ◽  
Ferida Esho ◽  
Aidan Lavery ◽  
Michael G. B. Drew
Keyword(s):  
Macrocyclic Ligand ◽  
Copper Proteins ◽  
Type 3 ◽  
Dicopper Complexes

Emission spectra from copper proteins containing type-3 centres

1983 ◽  
Vol 17 (2) ◽  
pp. 125-130 ◽  
Author(s):  
M. Bacci ◽  
M.G. Baldecchi ◽  
P. Fabeni ◽  
R. Linari ◽  
G.P. Pazzi
Keyword(s):  
Emission Spectra ◽  
Copper Proteins ◽  
Type 3

scholarly journals Determination of tyrosinase substrate-binding modes reveals mechanistic differences between type-3 copper proteins

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Mor Goldfeder ◽  
Margarita Kanteev ◽  
Sivan Isaschar-Ovdat ◽  
Noam Adir ◽  
Ayelet Fishman
Keyword(s):  
Substrate Binding ◽  
Copper Proteins ◽  
Binding Modes ◽  
Type 3

Human 3α-hydroxysteroid dehydrogenase type 3: structural clues of 5α-DHT reverse binding and enzyme down-regulation decreasing MCF7 cell growth

2016 ◽  
Vol 473 (8) ◽  
pp. 1037-1046 ◽  
Author(s):  
Bo Zhang ◽  
Xiao-Jian Hu ◽  
Xiao-Qiang Wang ◽  
Jean-François Thériault ◽  
Dao-Wei Zhu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Crystal Structure ◽  
Cell Growth ◽  
Mcf7 Cell ◽  
Hydroxysteroid Dehydrogenase ◽  
Cancer Cell Growth ◽  
Down Regulation ◽  
Breast Cancer Cell Growth ◽  
Type 3 ◽  
First Time

Human 3α-HSD3 (3α-hydroxysteroid dehydrogenase type 3) plays an essential role in the inactivation of the most potent androgen 5α-DHT (5α-dihydrotestosterone). The present study attempts to obtain the important structure of 3α-HSD3 in complex with 5α-DHT and to investigate the role of 3α-HSD3 in breast cancer cells. We report the crystal structure of human 3α-HSD3·NADP+·A-dione (5α-androstane-3,17-dione)/epi-ADT (epiandrosterone) complex, which was obtained by co-crystallization with 5α-DHT in the presence of NADP+. Although 5α-DHT was introduced during the crystallization, oxidoreduction of 5α-DHT occurred. The locations of A-dione and epi-ADT were identified in the steroid-binding sites of two 3α-HSD3 molecules per crystal asymmetric unit. An overlay showed that A-dione and epi-ADT were oriented upside-down and flipped relative to each other, providing structural clues for 5α-DHT reverse binding in the enzyme with the generation of different products. Moreover, we report the crystal structure of the 3α-HSD3·NADP+·4-dione (4-androstene-3,17-dione) complex. When a specific siRNA (100 nM) was used to suppress 3α-HSD3 expression without interfering with 3α-HSD4, which shares a highly homologous active site, the 5α-DHT concentration increased, whereas MCF7 cell growth was suppressed. The present study provides structural clues for 5α-DHT reverse binding within 3α-HSD3, and demonstrates for the first time that down-regulation of 3α-HSD3 decreases MCF7 breast cancer cell growth.

scholarly journals The putative polysaccharide deacetylase Ba0331: cloning, expression, crystallization and structure determination

2019 ◽  
Vol 75 (4) ◽  
pp. 312-320
Author(s):  
Athena Andreou ◽  
Petros Giastas ◽  
Sofia Arnaouteli ◽  
Mary Tzanodaskalaki ◽  
Socrates J. Tzartos ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Comparative Analysis ◽  
Bacillus Anthracis ◽  
Structure Determination ◽  
Cell Shape ◽  
Catalytic Domain ◽  
Extreme Conditions ◽  
Carbohydrate Esterase ◽  
Type 3 ◽  
Fibronectin Type

Ba0331 is a putative polysaccharide deacetylase from Bacillus anthracis, the etiological agent of the disease anthrax, that contributes to adaptation of the bacterium under extreme conditions and to maintenance of the cell shape. In the present study, the crystal structure of Ba0331 was determined at 2.6 Å resolution. The structure consists of two domains: a fibronectin type 3-like (Fn3-like) domain and a NodB catalytic domain. The latter is present in all carbohydrate esterase family 4 enzymes, while a comparative analysis of the Fn3-like domain revealed structural plasticity despite the retention of the conserved Fn3-like domain characteristics.

Monooxygenase Activity of Type 3 Copper Proteins

2007 ◽  
Vol 40 (7) ◽  
pp. 592-600 ◽  
Author(s):  
Shinobu Itoh ◽  
Shunichi Fukuzumi
Keyword(s):  
Copper Proteins ◽  
Monooxygenase Activity ◽  
Type 3

Monooxygenase Activity of Type 3 Copper Proteins

ChemInform ◽  
2007 ◽  
Vol 38 (41) ◽  
Author(s):  
Shinobu Itoh ◽  
Shunichi Fukuzumi
Keyword(s):  
Copper Proteins ◽  
Monooxygenase Activity ◽  
Type 3
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