scholarly journals Crystal structure of the YjgF/YER057c/UK114 family protein from the hyperthermophilic archaeon Sulfolobus tokodaii strain 7

2005 ◽  
Vol 62 (2) ◽  
pp. 557-561 ◽  
Author(s):  
Takuya Miyakawa ◽  
Woo Cheol Lee ◽  
Ken-ichi Hatano ◽  
Yusuke Kato ◽  
Yoriko Sawano ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Tokodaii ◽  
Hyperthermophilic Archaeon ◽  
Family Protein

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 ST2348, a CBS domain protein, from hyperthermophilic archaeon Sulfolobus tokodaii

2008 ◽  
Vol 375 (1) ◽  
pp. 124-128 ◽  
Author(s):  
Preethi Ragunathan ◽  
Thirumananseri Kumarevel ◽  
Yoshihiro Agari ◽  
Akeo Shinkai ◽  
Seiki Kuramitsu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sulfolobus Tokodaii ◽  
Hyperthermophilic Archaeon ◽  
Cbs Domain ◽  
Domain Protein

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 a Plant Multidrug and Toxic Compound Extrusion Family Protein

Structure ◽  
2017 ◽  
Vol 25 (9) ◽  
pp. 1455-1460.e2 ◽  
Author(s):  
Yoshiki Tanaka ◽  
Shigehiro Iwaki ◽  
Tomoya Tsukazaki
Keyword(s):  
Crystal Structure ◽  
Toxic Compound ◽  
Family Protein

scholarly journals Crystal structure of a YeeE/YedE family protein engaged in thiosulfate uptake

2020 ◽  
Vol 6 (35) ◽  
pp. eaba7637
Author(s):  
Yoshiki Tanaka ◽  
Kunihito Yoshikaie ◽  
Azusa Takeuchi ◽  
Muneyoshi Ichikawa ◽  
Tomoyuki Mori ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sulfur Cycle ◽  
Sulfur Source ◽  
Bacterial Membrane ◽  
Density Maps ◽  
Family Protein ◽  
Cysteine Synthesis ◽  
Plausible Mechanism ◽  
Dynamics Simulations ◽  
Positively Charged

We have demonstrated that a bacterial membrane protein, YeeE, mediates thiosulfate uptake. Thiosulfate is used for cysteine synthesis in bacteria as an inorganic sulfur source in the global biological sulfur cycle. The crystal structure of YeeE at 2.5-Å resolution reveals an unprecedented hourglass-like architecture with thiosulfate in the positively charged outer concave side. YeeE is composed of loops and 13 helices including 9 transmembrane α helices, most of which show an intramolecular pseudo 222 symmetry. Four characteristic loops are buried toward the center of YeeE and form its central region surrounded by the nine helices. Additional electron density maps and successive molecular dynamics simulations imply that thiosulfate can remain temporally at several positions in the proposed pathway. We propose a plausible mechanism of thiosulfate uptake via three important conserved cysteine residues of the loops along the pathway.

Crystal structure of the cytosolic domain of the cation diffusion facilitator family protein

2009 ◽  
Vol 76 (3) ◽  
pp. 768-771 ◽  
Author(s):  
Takashi Higuchi ◽  
Motoyuki Hattori ◽  
Yoshiki Tanaka ◽  
Ryuichiro Ishitani ◽  
Osamu Nureki
Keyword(s):  
Crystal Structure ◽  
Cation Diffusion ◽  
Cation Diffusion Facilitator ◽  
Family Protein ◽  
Cytosolic Domain ◽  
Cation Diffusion Facilitator Family

Crystal structure of UDP-galactose 4-epimerase from the hyperthermophilic archaeon Pyrobaculum calidifontis

2011 ◽  
Vol 512 (2) ◽  
pp. 126-134 ◽  
Author(s):  
Haruhiko Sakuraba ◽  
Tomoyuki Kawai ◽  
Kazunari Yoneda ◽  
Toshihisa Ohshima
Keyword(s):  
Crystal Structure ◽  
Hyperthermophilic Archaeon ◽  
Pyrobaculum Calidifontis

scholarly journals Crystal structure of archaeal phosphopantothenate synthetase

2014 ◽  
Vol 70 (a1) ◽  
pp. C455-C455
Author(s):  
Akiko Kita ◽  
Asako Kishimoto ◽  
Takuya Ishibashi ◽  
Hiroya Tomita ◽  
Yuusuke Yokooji ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Sites ◽  
Catalytic Mechanism ◽  
Rotation Axis ◽  
Structural Features ◽  
Common Pathway ◽  
Hyperthermophilic Archaeon ◽  
Pantothenate Synthetase ◽  
Almost All ◽  
Coenzyme A Biosynthesis

Bacteria/eukaryotes share a common pathway for coenzyme A biosynthesis which involves two enzymes, pantothenate synthetase and pantothenate kinase, to convert pantoate to 4'-phosphopantothenate. These two enzymes are absent in almost all archaea. Recently, it was reported that two novel enzymes, pantoate kinase (PoK) and phosphopantothenate synthetase (PPS), are responsible for this conversion in archaea[1]. In archaea, pantoate is phosphorylated by PoK to produce 4-phosphopantoate (PPo), and then condensation of PPo and β-alanine is catalyzed by PPS, generating 4'-phosphopantothenate. Here, we report the crystal structure of PPS from the hyperthermophilic archaeon, Thermococcus kodakarensis and its complexes with ATP, and ATP and 4-phosphopantoate (PPo). PPS forms an asymmetric homodimer, in which two monomers composing a dimer, deviated from the exact 2-fold symmetry, displaying 40-130distortion. Two active sites in PPS dimer are located near the rotation axis. Due to the asymmetricity of PPS dimer molecule, two active sites in PPS dimer are not equivalent. The structural features are consistent with the mutagenesis data and the results of biochemical experiments previously reported. Based on the structures of PPS, PPS/ATP complex, and PPS/ATP/PPo complex, we discuss the catalytic mechanism by which PPS produces phosphopantoyl adenylate (PPA), which is thought to be a reaction intermediate.

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