A Long Residence Time Enoyl-Reductase Inhibitor Explores an Extended Binding Region with Isoenzyme-Dependent Tautomer Adaptation and Differential Substrate-Binding Loop Closure

2021 ◽  
Vol 7 (4) ◽  
pp. 746-758
Author(s):  
Sandra Eltschkner ◽  
Josef Kehrein ◽  
Thien Anh Le ◽  
Shabnam Davoodi ◽  
Benjamin Merget ◽  
...  
Keyword(s):  
Residence Time ◽  
Reductase Inhibitor ◽  
Substrate Binding ◽  
Binding Region ◽  
Enoyl Reductase ◽  
Loop Closure ◽  
Binding Loop

Reshaping the substrate binding region of (R)-selective ω-transaminase for asymmetric synthesis of (R)-3-amino-1-butanol

2020 ◽  
Vol 104 (9) ◽  
pp. 3959-3969 ◽  
Author(s):  
Xinxing Gao ◽  
Xin Zhang ◽  
Nianqing Zhu ◽  
Yi Mou ◽  
Hailing Zhang ◽  
...  
Keyword(s):  
Asymmetric Synthesis ◽  
Substrate Binding ◽  
Binding Region

scholarly journals Not Cleaving the His-tag of Thal Results in More Tightly Packed and Better-Diffracting Crystals

Crystals ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 1135
Author(s):  
Ann-Christin Moritzer ◽  
Tina Prior ◽  
Hartmut H. Niemann
Keyword(s):  
Active Site ◽  
Flavin Adenine Dinucleotide ◽  
Substrate Binding ◽  
Environmentally Friendly ◽  
Space Group ◽  
Cofactor Binding ◽  
Closed Conformation ◽  
His Tag ◽  
Halide Salts ◽  
Binding Loop

Flavin-dependent halogenases chlorinate or brominate their substrates in an environmentally friendly manner, only requiring the cofactor reduced flavin adenine dinucleotide (FADH2), oxygen, and halide salts. The tryptophan 6-halogenase Thal exhibits two flexible loops, which become ordered (substrate-binding loop) or adopt a closed conformation (FAD loop) upon substrate or cofactor binding. Here, we describe the structure of NHis-Thal-RebH5 containing an N-terminal His-tag from pET28a, which crystallized in a different space group (P21) and, surprisingly, diffracted to a higher resolution of 1.63 Å than previously deposited Thal structures (P64; ~2.2 Å) with cleaved His-tag. Interestingly, the binding of glycine in the active site can induce an ordered conformation of the substrate-binding loop.

Use of adenosine(5')polyphospho(5')pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli B

Biochemistry ◽  
1993 ◽  
Vol 32 (6) ◽  
pp. 1548-1554 ◽  
Author(s):  
Takao Hibi ◽  
Hiroaki Kato ◽  
Takaaki Nishioka ◽  
Junichi Oda ◽  
Hiroshi Yamaguchi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Substrate Binding ◽  
Glutathione Synthetase ◽  
Binding Region ◽  
Escherichia Coli B

scholarly journals Structural dynamics of lytic polysaccharide monoxygenases reveals a highly flexible substrate binding region

2019 ◽  
Vol 88 ◽  
pp. 1-10 ◽  
Author(s):  
Radhika Arora ◽  
Priya Bharval ◽  
Sheena Sarswati ◽  
Taner Z. Sen ◽  
Ragothaman M. Yennamalli
Keyword(s):  
Structural Dynamics ◽  
Substrate Binding ◽  
Flexible Substrate ◽  
Binding Region

scholarly journals A Divergent Substrate-Binding Loop within the Pro-oncogenic Protein Anterior Gradient-2 Forms a Docking Site for Reptin

2010 ◽  
Vol 404 (3) ◽  
pp. 418-438 ◽  
Author(s):  
Magdalena M. Maslon ◽  
Roman Hrstka ◽  
Borek Vojtesek ◽  
Ted R. Hupp
Keyword(s):  
Substrate Binding ◽  
Docking Site ◽  
Oncogenic Protein ◽  
Binding Loop
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