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TitleComprehensive analysis of protein-protein interactions between MbtH-like protein FscK and adenylation domains in nonribosomal biosynthesis of Fuscachelins.
Journal, issue, pagesTo Be Published
Publish dateAug 2, 2018 (structure data deposition date)
AuthorsBruner, S.D. / Zagulyaeva, A.A.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.65 - 1.85 Å
Structure data

PDB-6ea3:
Thermobifida fusca FscH adenylation domain complexed with MbtH-like protein FscK and Ser-AMP
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6eby:
Crystal structure of the MbtH-like protein FscK bound to the interface forming region of FscH adenylation domain from Thermobifida fusca
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-SRP:
SERYL ADENYLATE

ChemComp-HOH:
WATER

Source
  • thermobifida fusca (strain yx) (bacteria)
KeywordsLIGASE / siderophore biosynthesis / serine activating adenylation domain / MbtH-like protein / seryl-adenylate / PROTEIN BINDING / adenylation domain / domain activation

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