Study of multi-muon events produced in p\bar{p} interactions at \sqrt{s}=1.96 TeV

68 pages, 46 figures, 11 tables. Submitted to Phys. Rev. D. Removed typos from the authors' listWe report the results of a study of multi-muon events produced at the Fermilab Tevatron collider and acquired with the CDF II detector using a dedicated dimuon trigger. The production cross section and kinematics of events in which both muon candidates are produced inside the beam pipe of radius 1.5 cm are successfully modeled by known processes which include heavy flavor production. In contrast, we are presently unable to fully account for the number and properties of the remaining events, in which at least one muon candidate is produced outside of the beam pipe, in terms of the same understanding of the CDF II detector, trigger, and event reconstruction.Peer reviewe

LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3

Cellular uptake of vitamin A, production of visual chromophore, and triglyceride homeostasis in adipocytes depend on two representatives of the vertebrate N1pC/P60 protein family, lecithin:retinol acyltransferase (LRAT) and HRAS-like tumor suppressor 3 (HRASLS3). Both proteins function as lipid-metabolizing enzymes but differ in their substrate preferences and dominant catalytic activity. The mechanism of this catalytic diversity is not understood. Here, by using a gain-of-function approach, we identified a specific sequence responsible for the substrate specificity of N1pC/P60 proteins. A 2.2 Å crystal structure of HRASLS3/LRAT chimeric enzyme in a thioester catalytic intermediate state revealed a major structural rearrangement accompanied by 3D-domain swapping dimerization not observed in native HRASLS proteins. Structural changes affecting the active site environment contributed to slower hydrolysis of the catalytic intermediate supporting efficient acyl transfer. These findings reveal structural adaption that facilitates selective catalysis and mechanism responsible for diverse substrate specificity within the LRAT-like enzyme family