A computationally designed β-amino acid-containing miniprotein

2021 ◽  
Author(s):  
Magdalena Bejger ◽  
Paulina Fortuna ◽  
Magda Drewniak ◽  
Jacek Plewka ◽  
Wojciech Rypniewski ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Hydrophobic Core ◽  
Sequence Pattern ◽  
Compact Conformation

A new miniprotein built from three helices, including one structure based on a ααβαααβ sequence pattern was developed. Its crystal structure revealed a compact conformation with a well-packed hydrophobic core...

scholarly journals Crystal structure of Aspergillus fumigatus AroH , an aromatic amino acid aminotransferase

2021 ◽  
Author(s):  
Sharon Spizzichino ◽  
Gioena Pampalone ◽  
Mirco Dindo ◽  
Agostino Bruno ◽  
Luigina Romani ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Aspergillus Fumigatus ◽  
Aromatic Amino Acid ◽  
Aromatic Amino Acid Aminotransferase

The first 3′:5′-cyclic nucleotide–amino acid complex:L-His–cIMP

2012 ◽  
Vol 68 (8) ◽  
pp. o311-o316 ◽  
Author(s):  
Katarzyna Ślepokura
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Cyclic Nucleotide ◽  
Phosphate Group ◽  
Specific Amino Acid ◽  
Π Stacking ◽  
Cyclic Phosphate ◽  
Nucleotide Recognition ◽  
Group Play ◽  
Phosphate Groups

In the crystal structure of the L-His–cIMP complex,i.e.L-histidinium inosine 3′:5′-cyclic phosphate [systematic name: 5-(2-amino-2-carboxyethyl)-1H-imidazol-3-ium 7-hydroxy-2-oxo-6-(6-oxo-6,9-dihydro-1H-purin-9-yl)-4a,6,7,7a-tetrahydro-4H-1,3,5,2λ5-furo[3,2-d][1,3,2λ5]dioxaphosphinin-2-olate], C6H10N3O2+·C10H10N4O7P−, the Hoogsteen edge of the hypoxanthine (Hyp) base of cIMP and the Hyp face are engaged in specific amino acid–nucleotide (His...cIMP) recognition,i.e.by abutting edge-to-edge and by π–π stacking, respectively. The Watson–Crick edge of Hyp and the cIMP phosphate group play a role in nonspecific His...cIMP contacts. The interactions between the cIMP anions (anti/C3′–endo/trans–gauche/chair conformers) are realized mainly between riboses and phosphate groups. The results for this L-His–cIMP complex, compared with those for the previously reported solvated L-His–IMP crystal structure, indicate a different nature of amino acid–nucleotide recognition and interactions upon the 3′:5′-cyclization of the nucleotide phosphate group.

Reactivities of Piperazine-2,5-diones in Radical Bromination Reactions

1996 ◽  
Vol 49 (11) ◽  
pp. 1229 ◽  
Author(s):  
CLL Chai ◽  
DCR Hockless ◽  
AR King
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Chemical Reactivity ◽  
Trans Isomers ◽  
Radical Bromination ◽  
Conformational Effects ◽  
Cis And Trans Isomers ◽  
The Difference ◽  
Cis And Trans

The reactivities of various N,N'- diacetylated piperazine-2,5-diones towards radical bromination reactions are reported. The studies show that glycyl centres of piperazine-2,5-diones are more reactive towards radical bromination reactions compared to α-substituted amino acid centres. In addition, large differences in reactivities were observed for the cis and trans isomers of N,N'-diacetylated alanine anhydride. Single-crystal structure determination of each isomer revealed that conformational effects may account for the difference in chemical reactivity.

Mechanism of ligand binding – PDZ domain taken as example

2017 ◽  
Vol 13 (4) ◽  
Author(s):  
Dawid Dułak ◽  
Mateusz Banach ◽  
Zdzisław Wiśniowski ◽  
Leszek Konieczny ◽  
Irena Roterman
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Ion Channel ◽  
Pdz Domain ◽  
Traditional Model ◽  
Beta Sheet ◽  
Hydrophobic Core ◽  
Beta Strand ◽  
Model Based ◽  
Specific Ligand

AbstractThe mechanism of specific ligand binding by proteins is discussed using the PDZ domain complexing the pentapeptide. This process is critical for clustering the membrane ion channel. The traditional model based on the Beta-sheet extension by complexed pentapeptide is interpreted as a hydrophobic core extension supported by additional Beta-strand generated by complexed pentapeptide. The explanation is based on the fuzzy oil drop model applied to the crystal structure of PDZ-pentapeptide.

scholarly journals The crystal structure of a xyloglucan-specific endo-β-1,4-glucanase from Geotrichum sp. M128 xyloglucanase reveals a key amino acid residue for substrate specificity

FEBS Journal ◽  
2009 ◽  
Vol 276 (18) ◽  
pp. 5094-5100 ◽  
Author(s):  
Katsuro Yaoi ◽  
Hidemasa Kondo ◽  
Ayako Hiyoshi ◽  
Natsuko Noro ◽  
Hiroshi Sugimoto ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Amino Acid Residue
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