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. 2018 May 22;13(6):1438–1446. doi: 10.1021/acschembio.8b00276

Table 1. Comparison of Proteins with Shape-Shifting Behavior.

  Structure 1 Structure 1 PDB ID Structure 1 function Structure 2 Structure 2 PDB ID Structure 2 Function/ Activity
IscU S (Structured) State: 4 α-helices, 3 β-strands 24LX Interaction with DnaJ-type co-chaperone (HscB) D (Dis-ordered) State: Dynamically disordered N/A Cysteine desulfurase (IscS) binding
CLIC1 α3+β4 N-terminal domain, soluble, monomeric 1K0M Unknown All-α N-terminal domain, oligomeric, membrane-associated 1RK4 Chloride ion channel
RfaH “Closed” state: all-α fold, interdomain salt bridge 2OUG Auto-inhibition restricts recruitment to selected targets “Open” state: all-β fold, no salt bridge 2LCL Interacts with RNAP and the ribosome to inhibit termination and activate translation
Selecase slc1: Monomeric, active form 4QHF Metallo-peptidase slc4: Tetrameric, inactive form 4QHH Unknown
Mad2 O-Mad2: Open conformation 1DUJ Under investigation; required for full Mad-2 function C-Mad2: Closed conformation 1S2H Spindle Assembly Checkpoint (Cdc20 trapping)
Arc/ Switch Arc Arc: β-strand homodimer 1BDT Binds DNA and represses transcription Switch Arc: engineered variant of Arc with a helix replacing the β-strand 1QTG N/A
XCL1 Chemokine structure 1J9O Chemokine receptor binding β-sheet structure 2N54 Glycosamino-glycan binding