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Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3.

Abstract：

:Interactions between loops 2, 2' and 4, known as the loop bundle, stabilize the active site of caspase-3. Loop 4 (L4) is of particular interest due to its location between the active site and the dimer interface. We have disrupted a salt bridge between K242 and E246 at the base of L4 to determine its role in overall conformational stability and in maintaining the active site environment. Stability measurements show that only the K242A single mutant decreases stability of the dimer, whereas both single mutants and the double mutant demonstrate much lower activity compared to wild-type caspase-3. Structural studies of the caspase-3 variants show the involvement of K242 in hydrophobic interactions that stabilize helix 5, near the dimer interface, and the role of E246 appears to be to neutralize the positive charge of K242 within the hydrophobic cluster. Overall, the results suggest E246 and K242 are important in procaspase-3 for their interaction with neighboring residues, not with one another. Conversely, formation of the K242-E246 salt bridge in caspase-3 is needed for an accurate, stable conformation of loop L4 and proper active site formation in the mature enzyme.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Walters J,Swartz P,Mattos C,Clark AC

doi

10.1016/j.abb.2011.01.011

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

31-8

issue

1

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(11)00032-4

journal_volume

508

pub_type

杂志文章

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