Literature summary for 3.5.2.6 extracted from

Hanes, M.; Reynolds, K.; Mcnamara, C.; Ghosh, P.; Bonomo, R.; Kirsch, J.; Handel, T.
Specificity and cooperativity at beta-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions (2011), Proteins Struct. Funct. Bioinform., 79, 1267-1276.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Klebsiella pneumoniae

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the complex of SHV-1 mutant D104E with beta-lactamse inhibitor protein BLIP, to 1.6 A resolution. Mutation D104E results in a 1000fold enhancement in binding affinity to BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions	Klebsiella pneumoniae

Crystallization (Comment)

Organism

crystal structure of the complex of SHV-1 mutant D104E with beta-lactamse inhibitor protein BLIP, to 1.6 A resolution. Mutation D104E results in a 1000fold enhancement in binding affinity to BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions

Klebsiella pneumoniae

Protein Variants

Protein Variants	Comment	Organism
D104E	mutation results in a 1000fold enhancement in binding affinity to beta-lactamase inhibitor protein BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions	Klebsiella pneumoniae

Organism

Organism	UniProt	Comment	Textmining
Klebsiella pneumoniae	P0AD64	-	-

Synonyms

Synonyms	Comment	Organism
SHV-1	-	Klebsiella pneumoniae

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Release 2023.1 (January 2023)