An Amino Acid Residue (S201) in the Retinal Binding Pocket Regulates the Photoreaction Pathway of Phoborhodopsin

Biochemistry ◽  
2011 ◽  
Vol 50 (33) ◽  
pp. 7177-7183 ◽  
Author(s):  
Gang Dai ◽  
Yu Zhang ◽  
Jun Tamogami ◽  
Makoto Demura ◽  
Naoki Kamo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Binding Pocket ◽  
Retinal Binding Pocket

Tetranectin-Binding Site on Plasminogen Kringle 4 Involves the Lysine-Binding Pocket and at Least One Additional Amino Acid Residue†

Biochemistry ◽  
2000 ◽  
Vol 39 (25) ◽  
pp. 7414-7419 ◽  
Author(s):  
Jonas H. Graversen ◽  
Bent W. Sigurskjold ◽  
Hans C. Thøgersen ◽  
Michael Etzerodt
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Binding Pocket ◽  
Additional Amino Acid

scholarly journals Endocrine Disruption: Structural Interactions of Androgen Receptor against Di(2-ethylhexyl) Phthalate and Its Metabolites

Toxics ◽  
2020 ◽  
Vol 8 (4) ◽  
pp. 115
Author(s):  
Mohd Amin Beg ◽  
Ishfaq Ahmad Sheikh
Keyword(s):  
Hydrogen Bonding ◽  
Androgen Receptor ◽  
Amino Acid ◽  
Amino Acid Residue ◽  
Parent Compound ◽  
Binding Pocket ◽  
Primary Metabolite ◽  
Binding Data ◽  
Available Information ◽  
Ethylhexyl Phthalate

Diethylhexyl phthalate (DEHP) is a commonly used plasticizer in the manufacture of polyvinyl chloride plastics for household and commercial use. DEHP is a ubiquitous ecocontaminant and causes developmental and reproductive problems in children and adults. After exposure, DEHP is metabolized by endogenous hydrolysis and oxidation into the primary metabolite, mono-(2-ethylhexyl) phthalate (MEHP), and the secondary metabolites, mono-(2-ethyl-5-hydroxhexyl)phthalate (5-OH-MEHP), mono-(2-ethyl-5-oxohexyl) phthalate (5-oxo-MEHP), mono-(2-ethyl-5-carboxypentyl) phthalate (5-cx-MEPP), and mono-[(2-carboxymethyl)hexyl] phthalate (2-cx-MMHP). Very few studies have been reported on the adverse effects of DEHP metabolites, and the available information indicates that the metabolites might also be equally or more active as compared to the parent compound. In the present study, induced fit docking was used for structural binding characterization of the above five DEHP metabolites with androgen receptor (AR) to predict the potential endocrine-disrupting effects of these metabolites in AR signaling. All the DEHP metabolites interacted with the ligand-binding pocket of AR forming amino-acid residue interactions, hydrogen bonding, and pi-pi interactions. The binding energy of DEHP with AR was similar to that of native ligand testosterone. The amino-acid residue interactions of DEHP metabolites had 91–100% similarity compared to that of testosterone. In addition, all the DEHP metabolites and testosterone showed a common hydrogen bonding interaction with amino-acid Arg-752 of AR. Taken together, the structural binding data in the present study suggested the potential for DEHP metabolites to disrupt AR signaling, which may lead to androgen-related reproductive dysfunction.

scholarly journals Exchange of a single amino acid residue in the cryptophyte phycobiliprotein lyase GtCPES expands its substrate specificity

2020 ◽  
Author(s):  
Natascha Tomazic ◽  
Kristina E. Overkamp ◽  
Marco Aras ◽  
Antonio J. Pierik ◽  
Eckhard Hofmann ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Light Harvesting ◽  
Functional Characterization ◽  
Binding Pocket ◽  
Covalent Attachment ◽  
Single Amino Acid ◽  
Oxygenic Photosynthesis ◽  
Single Amino Acid Residue

ABSTRACTCryptophyte algae are among the few eukaryotes that employ phycobiliproteins (PBP) for light harvesting during oxygenic photosynthesis. In contrast to the cyanobacterial PBP that are organized in large membrane-associated super complexes, the phycobilisomes, those from cryptophytes are soluble within the chloroplast thylakoid lumen. Their light-harvesting capacity is due to covalent linkage of several open-chain tetrapyrrole chromophores (phycobilins). Guillardia theta utilizes the PBP phycoerythrin PE545 with 15,16-dihydrobiliverdin (DHBV) in addition to phycoerythrobilin (PEB) as chromophores. Thus far, the assembly of cryptophyte PBPs is not yet completely understood but involves the action of PBP-lyases as shown for cyanobacterial PBP. PBP-lyases facilitate the attachment of the chromophore in the right configuration and stereochemistry. Here we present the functional characterization of eukaryotic S-type PBP lyase GtCPES from G. theta. We show GtCPES mediated transfer and covalent attachment of PEB to the conserved Cys82 of the acceptor PBP β-subunit (PmCpeB) of Prochlorococcus marinus MED4. Based on the previously solved crystal structure, the GtCPES binding pocket was investigated using site-directed mutagenesis. Thereby, amino acid residues involved in phycobilin binding and transfer were identified. Interestingly, exchange of a single amino acid residue Met67 to Ala extended the substrate specificity to phycocyanobilin (PCB) likely by enlarging the substrate-binding pocket. Variant GtCPES_M67A binds both PEB and PCB forming a stable, colorful complex in vitro and in vivo produced in Escherichia coli. GtCPES_M67A is able to mediate PCB transfer to Cys82 of PmCpeB. Based on our data we postulate that a single amino acid residue determines the bilin-specificity of phycoerythrin S-type lyases but that additional factors regulate hand over to the target protein.

scholarly journals Kinetic characterization of yeast alcohol dehydrogenases. Amino acid residue 294 and substrate specificity.

1987 ◽  
Vol 262 (8) ◽  
pp. 3754-3761
Author(s):  
A.J. Ganzhorn ◽  
D.W. Green ◽  
A.D. Hershey ◽  
R.M. Gould ◽  
B.V. Plapp
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue ◽  
Kinetic Characterization ◽  
Alcohol Dehydrogenases

scholarly journals Amino Acid Residue at the 165th Position Tunes Eyfp Chromophore Maturation. A Structure-Based Design

2021 ◽  
Author(s):  
Nadya V. Pletneva ◽  
Eugene G. Maksimov ◽  
Elena A. Protasova ◽  
Anastasia V. Mamontova ◽  
Tatiana R. Simonyan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue
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