Insights into Positive and Negative Requirements for Protein–Protein Interactions by Crystallographic Analysis of the β-Lactamase Inhibitory Proteins BLIP, BLIP-I, and BLP

Gretes, Michael; Lim, Daniel; Castro, Liza de; Jensen, Susan E.; Kang, Sung Gyun; Lee, Kye Joon; Strynadka, N.C.J.

doi:10.1016/j.jmb.2009.03.058

Cited by 34 publications

(37 citation statements)

References 65 publications

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“…Protein-protein interaction areas were determined using the PISA package (37). They were defined as one-half of the difference between the total accessible area in isolated monomers and that of the monomers assembled in the complex (38). Residues were considered interacting if any of the atoms were within 0.4 nm of each other, employing the CCP4i package (39).…”

Section: Methodsmentioning

confidence: 99%

Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7

Ionel

Velázquez-Muriel

Luque

et al. 2011

Journal of Biological Chemistry

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Maturation of dsDNA bacteriophages involves assembling the virus prohead from a limited set of structural components followed by rearrangements required for the stability that is necessary for infecting a host under challenging environmental conditions. Here, we determine the mature capsid structure of T7 at 1 nm resolution by cryo-electron microscopy and compare it with the prohead to reveal the molecular basis of T7 shell maturation. The mature capsid presents an expanded and thinner shell, with a drastic rearrangement of the major protein monomers that increases in their interacting surfaces, in turn resulting in a new bonding lattice. The rearrangements include tilting, in-plane rotation, and radial expansion of the subunits, as well as a relative bending of the A-and P-domains of each subunit. The unique features of this shell transformation, which does not employ the accessory proteins, inserted domains, or molecular interactions observed in other phages, suggest a simple capsid assembling strategy that may have appeared early in the evolution of these viruses.

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Section: Methodsmentioning

confidence: 99%

Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7

Ionel

Velázquez-Muriel

Luque

et al. 2011

Journal of Biological Chemistry

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“…␤-Lactamase inhibitory proteins (BLIPs), 2 including BLIP and BLIP-II, are inhibitors of class A ␤-lactamases and are produced from the soil bacterium Streptomyces (15)(16)(17)(18). BLIP inhibits class A ␤-lactamases with a wide range of affinities (subnanomolar to micromolar) and has been the focus of many structural, thermodynamic, and kinetic investigations (8, 11, 19 -23).…”

mentioning

confidence: 99%

Identification of the β-Lactamase Inhibitor Protein-II (BLIP-II) Interface Residues Essential for Binding Affinity and Specificity for Class A β-Lactamases

Brown¹,

Chow²,

Ruprecht³

et al. 2013

Journal of Biological Chemistry

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“…Interestingly, S. clavuligerus also produces the mechanism-based inhibitor, clavulanic acid, and so this organism produces both protein and small-molecule inhibitors of class A ␤-lactamases (14,15). More recently, other BLIPs have been discovered; they include BLIP-I, which is 37% identical to BLIP and has a similar protein fold, and BLIP-II, which is unrelated in sequence and structure to BLIP and BLIP-I (16)(17)(18).…”

mentioning

confidence: 99%

BLIP-II Is a Highly Potent Inhibitor of Klebsiella pneumoniae Carbapenemase (KPC-2)

Brown

Chow

Palzkill

2013

Antimicrob Agents Chemother

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ABSTRACTβ-Lactamase inhibitory protein II (BLIP-II) is a potent inhibitor of class A β-lactamases. KPC-2 is a class A β-lactamase that is capable of hydrolyzing carbapenems and has become a widespread source of resistance to these drugs for Gram-negative bacteria. Determination of association and dissociation rate constants for binding between BLIP-II and KPC-2 reveals a very tight interaction with a calculated (koff/kon) equilibrium dissociation constant of 76 fM (76 × 10−15M).

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Insights into Positive and Negative Requirements for Protein–Protein Interactions by Crystallographic Analysis of the β-Lactamase Inhibitory Proteins BLIP, BLIP-I, and BLP

Cited by 34 publications

References 65 publications

Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7

Molecular Rearrangements Involved in the Capsid Shell Maturation of Bacteriophage T7

Identification of the β-Lactamase Inhibitor Protein-II (BLIP-II) Interface Residues Essential for Binding Affinity and Specificity for Class A β-Lactamases

BLIP-II Is a Highly Potent Inhibitor of Klebsiella pneumoniae Carbapenemase (KPC-2)

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