scholarly journals Crystal structure of the short-chain flavin reductase HpaC from Sulfolobus tokodaii strain 7

2005 ◽  
Vol 81 (6) ◽  
pp. 229-232
Author(s):  
Masahiko OKAI ◽  
Norio KUDO ◽  
Koji NAGATA ◽  
Woo Cheol LEE ◽  
Masayuki KAMO ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Short Chain ◽  
Flavin Reductase ◽  
Sulfolobus Tokodaii

Crystal Structure of Archaeal Photolyase from Sulfolobus tokodaii with Two FAD Molecules: Implication of a Novel Light-harvesting Cofactor

2007 ◽  
Vol 365 (4) ◽  
pp. 903-910 ◽  
Author(s):  
Masahiro Fujihashi ◽  
Nobutaka Numoto ◽  
Yukiko Kobayashi ◽  
Akira Mizushima ◽  
Masanari Tsujimura ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Light Harvesting ◽  
Sulfolobus Tokodaii

scholarly journals Crystal structure of STS042, a stand-alone RAM module protein, from hyperthermophilic archaeon Sulfolobus tokodaii strain7

2008 ◽  
Vol 71 (3) ◽  
pp. 1557-1562 ◽  
Author(s):  
Ken-ichi Miyazono ◽  
Masanari Tsujimura ◽  
Yutaka Kawarabayasi ◽  
Masaru Tanokura
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Tokodaii ◽  
Hyperthermophilic Archaeon

Crystal structure of thioredoxin domain of ST2123 from thermophilic archaea Sulfolobus tokodaii strain7

2007 ◽  
Vol 69 (1) ◽  
pp. 204-208 ◽  
Author(s):  
Hua Ming ◽  
Yusuke Kato ◽  
Ken-ichi Miyazono ◽  
Kosuke Ito ◽  
Masayuki Kamo ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Tokodaii ◽  
Thermophilic Archaea

scholarly journals Crystal structure of glutamine receptor protein from Sulfolobus tokodaii strain 7 in complex with its effector l -glutamine: implications of effector binding in molecular association and DNA binding

2008 ◽  
Vol 36 (14) ◽  
pp. 4808-4820 ◽  
Author(s):  
Thirumananseri Kumarevel ◽  
Noboru Nakano ◽  
Karthe Ponnuraj ◽  
Subash C. B. Gopinath ◽  
Keiko Sakamoto ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Dna Binding ◽  
Molecular Association ◽  
Receptor Protein ◽  
Sulfolobus Tokodaii ◽  
Effector Binding

scholarly journals Crystal structures of bacterial flavin reductase GraD and its complex with NADH

2014 ◽  
Vol 70 (a1) ◽  
pp. C488-C488
Author(s):  
Takae Yamauchi ◽  
Tomomi Fujii ◽  
Masahiro Yoshida ◽  
Tadao Oikawa ◽  
Yasuo Hata
Keyword(s):  
Crystal Structure ◽  
Three Dimensional ◽  
Sole Source ◽  
Diffusion Method ◽  
Flavin Reductase ◽  
Cell Parameters ◽  
Ping Pong ◽  
Reservoir Solution ◽  
Complex Crystals ◽  
Rhizobium Sp

Rhizobium sp. strain MTP-10005 uses the aromatic compound γ-resorcylate as a sole source of carbon and energy for growth. Resorcinol hydroxylase, which converts resorcinol to hydroxyquinol, plays an important role in the aerobic microbial catabolism of γ-resorcylate. Resorcinol hydroxylase from Rhizobium sp. strain MTP-10005 is a two-component enzyme consisting of the reductase and the monooxygenase components. The reductase component (GraD) is an oxidoreductase containing a flavin molecule as a cofactor. GraD catalyzes the NADH-dependent reduction of free FAD according to a ping-pong bisubstrate-biproduct mechanism. The reduced FAD is then used by the monooxygenase component GraA to hydroxylate resorcinol to hydroxyquinol. We have determined the three-dimensional structures of recombinant GraD with a bound FAD and in complex with NAD. GraD was crystallized at 293 K by the sitting-drop vapour-diffusion method using a precipitant solution containing 13 - 14% (w/v) PEG 2000, 6 - 9% (v/v) 2-propanol, 100 mM sodium citrate pH 5.6, 100 mM DTT and 200 μM FAD. The approximate dimensions of the obtained crystals were 0.1 × 0.1 × 0.15 mm3. The crystal diffracted to 1.8Å and belongs to space group P41212 with unit-cell parameters of a = b = 77.8 Å and c = 124.2 Å. The crystal structure has been determined by the molecular replacement and refined at 1.8 Å resolution. GraD exists as a homodimer, and each monomer contains an FAD. The probable binding site for NADH is covered with the N-terminal sub-domain in chain A, whereas the site is completely exposed to bulk solvent in chain B. The NAD-complex crystals were prepared by soaking the GraD crystals in the reservoir solution supplemented with NADH. The crystal diffracted to 1.8 Å, and the crystal structure was determined at 1.8 Å resolution. The Fo-Fc maps for the crystal soaked with NADH showed the electron densities corresponding to the nicotinamide ring and the adenyl moiety in chain B.

scholarly journals Crystal Structure of Rat Short Chain Acyl-CoA Dehydrogenase Complexed with Acetoacetyl-CoA

2002 ◽  
Vol 277 (14) ◽  
pp. 12200-12207 ◽  
Author(s):  
Kevin P. Battaile ◽  
JoAnn Molin-Case ◽  
Rosemary Paschke ◽  
Ming Wang ◽  
Dennis Bennett ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Short Chain ◽  
Chain Acyl

scholarly journals The first crystal structure of an archaeal metallo-β-lactamase superfamily protein; ST1585 from Sulfolobus tokodaii

2010 ◽  
Vol 78 (10) ◽  
pp. 2399-2402 ◽  
Author(s):  
Atsuhiro Shimada ◽  
Hirohito Ishikawa ◽  
Noriko Nakagawa ◽  
Seiki Kuramitsu ◽  
Ryoji Masui
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Tokodaii
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