Prediction of the secondary and tertiary structures of interferon from four homologous amino acid sequences

Bile-salt activated carboxylic ester lipase (CEL) is a major triglyceride, cholesterol ester and vitamin ester hydrolytic enzyme contained within pancreatic and lactating mammary gland secretions. Bioinformatic methods were used to predict the amino acid sequences, secondary and tertiary structures and gene locations for CEL genes, and encoded proteins using data from several vertebrate genome projects. A proline-rich and O-glycosylated 11-amino acid C-terminal repeat sequence (VNTR) previously reported for human and other higher primate CEL proteins was also observed for other eutherian mammalian CEL sequences examined. In contrast, opossum CEL contained a single C-terminal copy of this sequence whereas CEL proteins from platypus, chicken, lizard, frog and several fish species lacked the VNTR sequence. Vertebrate CEL genes contained 11 coding exons. Evidence is presented for tandem duplicated CEL genes for the zebrafish genome. Vertebrate CEL protein subunits shared 53–97% sequence identities; demonstrated sequence alignments and identities for key CEL amino acid residues; and conservation of predicted secondary and tertiary structures with those previously reported for human CEL. Phylogenetic analyses demonstrated the relationships and potential evolutionary origins of the vertebrate CEL family of genes which were related to a nematode carboxylesterase (CES) gene and five mammalian CES gene families.

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Protein Tertiary Structures: Prediction from Amino Acid Sequences

Encyclopedia of Life Sciences ◽

10.1038/npg.els.0003040 ◽

2002 ◽

Cited By ~ 4

Author(s):

Hongyu Zhang

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Tertiary Structures

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Analyses of Amino Acid Sequences and Tertiary Structures among Ohr Enzymes Revealed a Catalytic Role for Y126

Free Radical Biology and Medicine ◽

10.1016/j.freeradbiomed.2016.10.067 ◽

2016 ◽

Vol 100 ◽

pp. S27

Author(s):

Diogo de Abreu Meireles ◽

Renato Mateus Domingos ◽

Thiago G Alegria ◽

Luis Eduardo Soares Netto

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Tertiary Structures ◽

Catalytic Role

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A distinct molecular signature on anhydrobiotic cyanobacterial metallothioneins

Research Society and Development ◽

10.33448/rsd-v10i2.12714 ◽

2021 ◽

Vol 10 (2) ◽

pp. e50610212714

Author(s):

Danyel Fernandes Contiliani ◽

Vitor Nolasco de Moraes ◽

Yasmin de Araújo Ribeiro ◽

Tiago Campos Pereira

Keyword(s):

Amino Acid ◽

Metal Ion ◽

Protein Structures ◽

Amino Acid Sequences ◽

Protein Stabilization ◽

Molecular Signature ◽

Tertiary Structures ◽

Cellular Protection ◽

Structural Superposition ◽

Clustal Omega

Anhydrobiosis refers to a state of suspended animation in which some organisms enter when exposed to extreme desiccation, ensuring them an outstanding tolerance to several physical stresses due to molecular and cellular adaptations. Metallothioneins (MTs) are short cysteine-rich metal-chelating proteins that work as a cellular protection element in metal ion-rich conditions. Here we aimed to investigate possible molecular signatures in primary and tertiary structures in anhydrobiotic cyanobacterial MTs. Anhydrobiotic and non-anhydrobiotic cyanobacterial MT amino acid sequences were retrieved from NCBI database and aligned in Clustal Omega server. Additionally, the amino acid compositions of these sequences were determined by GeneRunner. Further, we carried out homology-modeling via SWISS-MODEL, structural superposition in UCSF Chimera 1.4 Matchmaker tool and ligand-binding site prediction via COFACTOR. In silico analyses revealed specific divergences in amino acid positions between MT groups, evidencing positive and negative selections, however without affecting final protein structures. Some of these changes on polypeptide sequence potentially enhance protein stabilization during desiccation, whereas others possibly act as additional metal-ion coordinating residues. Analyses on the molecular adaptations on anhydrobiotic cyanobacterial MTs help shed light on their molecular functions and biological roles, as well as may have applications on the development of desiccation- and metal-tolerant organisms.

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Homologous amino acid sequences in enzymes mediating sequential metabolic reactions.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)34635-5 ◽

1978 ◽

Vol 253 (14) ◽

pp. 4920-4923

Author(s):

W.K. Yeh ◽

G. Davis ◽

P. Fletcher ◽

L.N. Ornston

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Metabolic Reactions ◽

Homologous Amino Acid

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Structural role of the tyrosine residues of cytochrome c

Biochemical Journal ◽

10.1042/bj2050153 ◽

1982 ◽

Vol 205 (1) ◽

pp. 153-165 ◽

Cited By ~ 18

Author(s):

C G Eley ◽

G R Moore ◽

R J Williams ◽

W Neupert ◽

P J Boon ◽

...

Keyword(s):

Amino Acid ◽

High Resolution ◽

Cytochrome C ◽

Amino Acid Sequences ◽

The Other ◽

Amino Acid Substitutions ◽

Tertiary Structures ◽

Tyrosine Residues ◽

Cytochromes C

The tertiary structures of horse, tuna, Neurospora crassa, horse [Hse65,Leu67]- and horse [Hse65,Leu74]-cytochromes c were studied with high-resolution 1H n.m.r. spectroscopy. The amino acid sequences of these proteins differ at position 46, which is occupied by phenylalanine in the horse proteins but by tyrosine in the remaining two, and at positions 67, 74 and 97, which are all occupied by tyrosine residues in horse and tuna cytochrome c but in the other proteins are substituted by phenylalanine or leucine, though there is only one such substitution per protein. The various aromatic-amino-acid substitutions do not seriously affect the protein structure.

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