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ACP modification to understand protein‐protein interactions in fatty acid biosynthesis (768.6)
Author(s) -
Burkart Michael
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.768.6
Subject(s) - acyl carrier protein , dehydratase , substrate (aquarium) , biochemistry , chemistry , enzyme , biosynthesis , protein subunit , protein–protein interaction , stereochemistry , biology , gene , ecology
In order to investigate protein‐protein interactions, we have developed a suite of tools to modify the ACP with substrate analogs and reactive probes. These ACP conjugates are used to study the structure of the ACP using NMR and x‐ray crystallography. The interaction between E. coli AcpP and its dehydratase FabA, we have captured both the dynamic and static interactions. These highlight the molecular events by which FabA binds and spreads alpha helices II and III of AcpP, releasing the bound substrate to enter the active site of the enzyme. These tools can be generally applied to any carrier protein dependent pathway, including PKS and NRPS systems. Grant Funding Source : NIH‐NIGMS