scholarly journals Amino Acid Insertion Reveals a Necessary Three-Helical Intermediate in the Folding Pathway of the Colicin E7 Immunity Protein Im7

2009 ◽  
Vol 392 (4) ◽  
pp. 1074-1086 ◽  
Author(s):  
Stuart E. Knowling ◽  
Angelo Miguel Figueiredo ◽  
Sara B.-M. Whittaker ◽  
Geoffrey R. Moore ◽  
Sheena E. Radford
Keyword(s):  
Amino Acid ◽  
Folding Pathway ◽  
Immunity Protein ◽  
Amino Acid Insertion ◽  
Colicin E7

Identification of a new 2‐amino acid insertion in the integrase coding region of HIV‐1 subtype G isolates

2021 ◽  
Author(s):  
João Pereira‐Vaz ◽  
Pedro Crespo ◽  
Luísa Mocho ◽  
Patrícia Martinho ◽  
Teresa Fidalgo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Coding Region ◽  
Amino Acid Insertion ◽  
Hiv 1

scholarly journals Humanizing the yeast origin recognition complex

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Clare S. K. Lee ◽  
Ming Fung Cheung ◽  
Jinsen Li ◽  
Yongqian Zhao ◽  
Wai Hei Lam ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Complex ◽  
Origin Recognition Complex ◽  
Specific Binding ◽  
Life Cycles ◽  
Amino Acid Insertion ◽  
Evolutionarily Conserved ◽  
Transcriptional Start Sites ◽  
Eukaryote Genome ◽  
Origin Recognition

AbstractThe Origin Recognition Complex (ORC) is an evolutionarily conserved six-subunit protein complex that binds specific sites at many locations to coordinately replicate the entire eukaryote genome. Though highly conserved in structure, ORC’s selectivity for replication origins has diverged tremendously between yeasts and humans to adapt to vastly different life cycles. In this work, we demonstrate that the selectivity determinant of ORC for DNA binding lies in a 19-amino acid insertion helix in the Orc4 subunit, which is present in yeast but absent in human. Removal of this motif from Orc4 transforms the yeast ORC, which selects origins based on base-specific binding at defined locations, into one whose selectivity is dictated by chromatin landscape and afforded with plasticity, as reported for human. Notably, the altered yeast ORC has acquired an affinity for regions near transcriptional start sites (TSSs), which the human ORC also favors.

scholarly journals Thyrotropin Receptor Cleavage at Site 1 Involves Two Discontinuous Segments at Each End of the Unique 50-Amino Acid Insertion

1999 ◽  
Vol 274 (4) ◽  
pp. 2093-2096 ◽  
Author(s):  
Kunihiko Tanaka ◽  
Gregorio D. Chazenbalk ◽  
Sandra M. McLachlan ◽  
Basil Rapoport
Keyword(s):  
Amino Acid ◽  
Thyrotropin Receptor ◽  
Amino Acid Insertion

scholarly journals KPC-50 Confers Resistance to Ceftazidime-Avibactam Associated with Reduced Carbapenemase Activity

2020 ◽  
Vol 64 (8) ◽  
Author(s):  
Laurent Poirel ◽  
Xavier Vuillemin ◽  
Mario Juhas ◽  
Amandine Masseron ◽  
Ursina Bechtel-Grosch ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Clinical Isolate ◽  
Sharp Reduction ◽  
Content Type ◽  
Amino Acid Insertion

ABSTRACT KPC-50 is a KPC-3 variant identified from a Klebsiella pneumoniae clinical isolate recovered in Switzerland in 2019. Compared to KPC-3, KPC-50 shows (i) a three-amino-acid insertion (Glu-Ala-Val) between amino acids 276 and 277, (ii) an increased affinity to ceftazidime, (iii) a decreased sensitivity to avibactam, explaining the ceftazidime-avibactam resistance, and (iv) an association with a sharp reduction of its carbapenemase activity.

Effect of an Amino Acid Insertion into the Omega Loop Region of a Class C β-Lactamase on Its Substrate Specificity†

Biochemistry ◽  
1998 ◽  
Vol 37 (29) ◽  
pp. 10461-10468 ◽  
Author(s):  
Michiyoshi Nukaga ◽  
Kazuo Taniguchi ◽  
Yukio Washio ◽  
Tetsuo Sawai
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Loop Region ◽  
Amino Acid Insertion ◽  
Omega Loop ◽  
Class C

scholarly journals Residues in the Apical Domain of the Feline and Canine Transferrin Receptors Control Host-Specific Binding and Cell Infection of Canine and Feline Parvoviruses

2003 ◽  
Vol 77 (16) ◽  
pp. 8915-8923 ◽  
Author(s):  
Laura M. Palermo ◽  
Karsten Hueffer ◽  
Colin R. Parrish
Keyword(s):  
Amino Acid ◽  
Specific Binding ◽  
Glycosylation Site ◽  
Single Amino Acid ◽  
Transferrin Receptors ◽  
Cell Infection ◽  
Feline Panleukopenia Virus ◽  
Amino Acid Insertion ◽  
Apical Domain ◽  
Mutant Receptors

ABSTRACT Canine parvovirus (CPV) and feline panleukopenia virus (FPV) capsids bind to the transferrin receptors (TfRs) of their hosts and use these receptors to infect cells. The binding is partially host specific, as FPV binds only to the feline TfR, while CPV binds to both the canine and feline TfRs. The host-specific binding is controlled by a combination of residues within a raised region of the capsid. To define the TfR structures that interact with the virus, we altered the apical domain of the feline or canine TfR or prepared chimeras of these receptors and tested the altered receptors for binding to FPV or CPV capsids. Most changes in the apical domain of the feline TfR did not affect binding, but replacing Leu221 with Ser or Asp prevented receptor binding to either FPV or CPV capsids, while replacing Leu221 with Lys resulted in a receptor that bound only to CPV but not to FPV. Analysis of recombinants of the feline and canine TfRs showed that sequences controlling CPV-specific binding were within the apical domain and that more than one difference between these receptors determined the CPV-specific binding of the canine TfR. Single changes within the canine TfR which removed a single amino acid insertion or which eliminated a glycosylation site gave that receptor the expanded ability to bind to FPV and CPV. In some cases, binding of capsids to mutant receptors did not result in infection, suggesting a structural role for the receptor in cell infection by the viruses.

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