Structure of Replication Protein A

Replication Protein A (RPA) has been studied extensively by many research groups and the tertiary structure of the protein has been characterized through NMR / X-ray diffraction experiments. What follows is a brief summary of these structural studies and our predictions for the remaining, structurally unresolved fragments of RPA.
 

Secondary Structure:
 

For the domains in RPA whose tertiary structure was available, the secondary structure and solvent accessibility was visualized using the POLYVIEW server. Otherwise, the secondary structure and solvent accessibility of amino acid residues were predicted using our SABLE protein structure prediction server. POLYVIEW was again used to combine the results.

Please click the links to view the results:  RPA14   ,   RPA32   ,   RPA70.

Tertiary structure:


The different entries in the Protein Data Bank are listed below.

       1. 1L1O : RPA trimerization core containing RPA70 C-terminal domain, RPA32 central domain and RPA14.

       2. 1JMC : RPA70 DNA binding domain bound to a DNA single-strand.

       3. 1FGU : RPA70 Central domain.

       4. 1QUQ : RPA32 Central domain and RPA14.

       5. 1DPU : RPA32 C-terminal domain bound to Uracil DNA Glycosylase (UNG2).

Note: For RPA14: Full tertiary structure (1L1O,1QUQ) has been determined.
          For RPA32: N-terminal structure is not clear. Central domain (1L1O,1QUQ) and C-terminal (1DPU) are available.
          For RPA70: N-terminal structure is not clear. Central domain (1JMC,1FGU) and C-terminal (1L1O) are available.

POLYVIEW representation of the trimeric core crystal structure 1L1O are included below. Residues in contact in the trimer are highlighted in magenta in chains A, B and C, respectively.

Chain A:

Chain B:

Chain C: