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Fig. 1 | BMC Biochemistry

Fig. 1

From: Systematic substitutions at BLIP position 50 result in changes in binding specificity for class A β-lactamases

Fig. 1

Structural representation of the interaction between BLIP and β-lactamases. BLIP is shown as a purple ribbon with Tyr50BLIP shown as stick. TEM-1 a and KPC-2 b β-lactamases are shown as white spheres with the catalytic Ser70 in yellow and positions 107, 129 and 216 (that make contact with Tyr50BLIP) are shown in red. PDB codes: 1JTG and 3E2K. Alignment of apo (gray) and bound (white) TEM-1 c and KPC-2 d structures shown in ribbon with position 105β-lactamase shown as stick. BLIPY50 is shown as a purple stick in the bound form. The measurement provides the distance 105β-lactamase moves upon binding to BLIP. PDB codes 1BTL and 2OV5 (apo) and 1JTG and 3E2K (bound). Images generated with Chimera

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BMC Biochemistry

ISSN: 1471-2091

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