A retractable lid in lecithin:cholesterol acyltransferase provides a structural mechanism for activation by apolipoprotein A-I

Manthei, Kelly A.; Ahn, Joomi; Glukhova, Alisa; Yuan, Wenmin; Larkin, Christopher; Manett, Taylor D.; Chang, Louise; Shayman, James A.; Axley, Milton J.; Schwendeman, Anna; Tesmer, John J. G.

doi:10.1074/jbc.M117.802736

Title: A retractable lid in lecithin:cholesterol acyltransferase provides a structural mechanism for activation by apolipoprotein A-I

Journal Article · 13 October 2017 · Journal of Biological Chemistry

DOI: https://doi.org/10.1074/jbc.M117.802736 · OSTI ID:1438877

Manthei, Kelly A. ^[1]; Ahn, Joomi ^[2]; Glukhova, Alisa ^[3]; Yuan, Wenmin ^[1]; Larkin, Christopher ^[2]; Manett, Taylor D. ^[1]; Chang, Louise ^[1]; Shayman, James A. ^[1]; Axley, Milton J. ^[2]; Schwendeman, Anna ^[1]; Tesmer, John J. G. ^[4]

Univ. of Michigan, Ann Arbor, MI (United States)
MedImmune, Gaithersburg, MD (United States)
Univ. of Michigan, Ann Arbor, MI (United States); Monash Univ., Parkville, VIC (Australia)
Univ. of Michigan, Ann Arbor, MI (United States); Purdue Univ., West Lafayette, IN (United States)

Lecithin:cholesterol acyltransferase (LCAT) plays a key role in reverse cholesterol transport by transferring an acyl group from phosphatidylcholine to cholesterol, promoting the maturation of high-density lipoproteins (HDL) from discoidal to spherical particles. LCAT is activated through an unknown mechanism by apolipoprotein A-I (apoA-I) and other mimetic peptides that form a belt around HDL. Here, we report the crystal structure of LCAT with an extended lid that blocks access to the active site, consistent with an inactive conformation. Residues Thr-123 and Phe-382 in the catalytic domain form a latch-like interaction with hydrophobic residues in the lid. Because these residues are mutated in genetic disease, lid displacement was hypothesized to be an important feature of apoA-I activation. Functional studies of site-directed mutants revealed that loss of latch interactions or the entire lid enhanced activity against soluble ester substrates, and hydrogen–deuterium exchange (HDX) mass spectrometry revealed that the LCAT lid is extremely dynamic in solution. Upon addition of a covalent inhibitor that mimics one of the reaction intermediates, there is an overall decrease in HDX in the lid and adjacent regions of the protein, consistent with ordering. As a result, these data suggest a model wherein the active site of LCAT is shielded from soluble substrates by a dynamic lid until it interacts with HDL to allow transesterification to proceed.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Inst. of Health; American Heart Assoc. Scientist Development Grant; American Heart Assoc. Postdoctoral Fellowship; Ruth L. Kirschstein NRSA

Grant/Contract Number:: HL071818; HL122416; AR056991; 13SDG17230049; 16POST27760002; 15POST24870001; F32HL131288

OSTI ID:: 1438877

Journal Information:: Journal of Biological Chemistry, Vol. 292, Issue 49; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 26 works

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
acyltransferase
apolipoprotein
cholesterol
conformational change
crystallography
high-density lipoprotein (HDL)
inhibitor
structural biology
HDX MS
lecithin

Title: A retractable lid in lecithin:cholesterol acyltransferase provides a structural mechanism for activation by apolipoprotein A-I

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