Hydrogenase enzymes: Recent structural studies and active site models

2009 ◽  
Vol 694 (17) ◽  
pp. 2671-2680 ◽  
Author(s):  
D. Michael Heinekey
Keyword(s):  
Active Site ◽  
Structural Studies ◽  
Hydrogenase Enzymes

Mutational and structural studies of the active-site residues in truncatedFibrobacter succinogenes1,3–1,4-β-D-glucanase

2008 ◽  
Vol 64 (12) ◽  
pp. 1259-1266 ◽  
Author(s):  
Li-Chu Tsai ◽  
Hsiao-Chuan Huang ◽  
Ching-Hua Hsiao ◽  
Yuan-Neng Chiang ◽  
Lie-Fen Shyur ◽  
...  
Keyword(s):  
Active Site ◽  
Structural Studies ◽  
Active Site Residues

RNA Splicing by the Spliceosome

2020 ◽  
Vol 89 (1) ◽  
pp. 359-388 ◽  
Author(s):  
Max E. Wilkinson ◽  
Clément Charenton ◽  
Kiyoshi Nagai
Keyword(s):  
Splice Site ◽  
Active Site ◽  
Rna Splicing ◽  
Messenger Rna ◽  
Structural Studies ◽  
U2 Snrna ◽  
U6 Snrna ◽  
Mature Mrna ◽  
Catalytic Metal ◽  
Small Nuclear Ribonucleoproteins

The spliceosome removes introns from messenger RNA precursors (pre-mRNA). Decades of biochemistry and genetics combined with recent structural studies of the spliceosome have produced a detailed view of the mechanism of splicing. In this review, we aim to make this mechanism understandable and provide several videos of the spliceosome in action to illustrate the intricate choreography of splicing. The U1 and U2 small nuclear ribonucleoproteins (snRNPs) mark an intron and recruit the U4/U6.U5 tri-snRNP. Transfer of the 5′ splice site (5′SS) from U1 to U6 snRNA triggers unwinding of U6 snRNA from U4 snRNA. U6 folds with U2 snRNA into an RNA-based active site that positions the 5′SS at two catalytic metal ions. The branch point (BP) adenosine attacks the 5′SS, producing a free 5′ exon. Removal of the BP adenosine from the active site allows the 3′SS to bind, so that the 5′ exon attacks the 3′SS to produce mature mRNA and an excised lariat intron.

Active Site of Lysyl-tRNA Synthetase:  Structural Studies of the Adenylation Reaction†

Biochemistry ◽  
2000 ◽  
Vol 39 (29) ◽  
pp. 8418-8425 ◽  
Author(s):  
Gianluigi Desogus ◽  
Flavia Todone ◽  
Peter Brick ◽  
Silvia Onesti
Keyword(s):  
Active Site ◽  
Trna Synthetase ◽  
Structural Studies

scholarly journals Crystallization and preliminary X-ray diffraction analysis of human DNA primase

2014 ◽  
Vol 70 (2) ◽  
pp. 206-210 ◽  
Author(s):  
Andrey G. Baranovskiy ◽  
Jianyou Gu ◽  
Nigar D. Babayeva ◽  
Vinod B. Agarkar ◽  
Yoshiaki Suwa ◽  
...  
Keyword(s):  
Active Site ◽  
Large Subunit ◽  
Structural Studies ◽  
Asymmetric Unit ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Human Dna ◽  
Structural Details

Human primase synthesizes RNA primers and transfers them to the active site of Pol α with subsequent extension with dNTPs. Human primase is a heterodimer of two subunits: a small catalytic subunit (p49) and a large subunit (p58). The structural details of the initiation and elongation steps of primer synthesis, as well as primer length counting, are not known. To address these questions, structural studies of human primase were initiated. Two types of crystals were obtained. The best diffracting crystals belonged to space groupP1, with unit-cell parametersa= 86.2,b= 88.9,c= 94.68 Å, α = 93.82, β = 96.57, γ = 111.72°, and contained two heterodimers of full-length p49 and p59 subunits in the asymmetric unit.

Synthetic and Structural Studies of Butterfly Fe/S/P Cluster Complexes Related to the Active Site of [FeFe]-Hydrogenases. Proton Reduction to H2Catalyzed by (η1-Ph2PS-η1)2Fe2(CO)6

2008 ◽  
Vol 27 (15) ◽  
pp. 3714-3721 ◽  
Author(s):  
Li-Cheng Song ◽  
Guang-Huai Zeng ◽  
Shao-Xia Lou ◽  
Hui-Ning Zan ◽  
Jiang-Bo Ming ◽  
...  
Keyword(s):  
Active Site ◽  
Structural Studies ◽  
Proton Reduction ◽  
Cluster Complexes

scholarly journals Structures of Human Transglutaminase 2: Finding Clues for Interference in Cross-linking Mediated Activity

2020 ◽  
Vol 21 (6) ◽  
pp. 2225
Author(s):  
Gi Eob Kim ◽  
Hyun Ho Park
Keyword(s):  
Neurodegenerative Disorders ◽  
Active Site ◽  
Drug Target ◽  
Structural Information ◽  
Transglutaminase 2 ◽  
Cross Linking ◽  
Targeted Drugs ◽  
Clinical Use ◽  
Structural Studies ◽  
Cellular Processes

Human transglutaminase 2 (TGase2) has various functions, including roles in various cellular processes such as apoptosis, development, differentiation, wound healing, and angiogenesis, and is linked to many diseases such as cancer. Although TGase2 has been considered an optimized drug target for the treatment of cancer, fibrosis, and neurodegenerative disorders, it has been difficult to generate TGase2-targeted drugs for clinical use because of the relatively flat and broad active site on TGase2. To design more specific and powerful inhibitors, detailed structural information about TGase2 complexed with various effector and inhibitor molecules is required. In this review, we summarized the current structural studies on TGase2, which will aid in designing drugs that can overcome the aforementioned limitations.

Sign in / Sign up

Export Citation Format

Share Document