1SRU

Crystal structure of full length E. coli SSB protein

Summary for 1SRU

• Entry DOI: 10.2210/pdb1sru/pdb
• Descriptor: Single-strand binding protein (1 entity in total)
• Functional Keywords: replication
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 50541.17

Authors

Savvides, S.N.,Raghunathan, S.,Fuetterer, K.,Kozlov, A.G.,Lohman, T.M.,Waksman, G. (deposition date: 2004-03-23, release date: 2004-08-03, Last modification date: 2024-02-14)

Primary citation

Savvides, S.N.,Raghunathan, S.,Fuetterer, K.,Kozlov, A.G.,Lohman, T.M.,Waksman, G.
The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA.
Protein Sci., 13:1942-1947, 2004

PubMed Abstract: The crystal structure of full-length homotetrameric single-stranded DNA (ssDNA)-binding protein from Escherichia coli (SSB) has been determined to 3.3 A resolution and reveals that the entire C-terminal domain is disordered even in the presence of ssDNA. To our knowledge, this is the first experimental evidence that the C-terminal domain of SSB may be inherently disordered. The N-terminal DNA-binding domain of the protein is well ordered and is virtually indistinguishable from the previously determined structure of the chymotryptic fragment of SSB (SSBc) in complex with ssDNA. The absence of observable interactions with the core protein and the crystal packing of SSB together suggest that the disordered C-terminal domains likely extend laterally away from the DNA- binding domains, which may facilitate interactions with components of the replication machinery in vivo. The structure also reveals the conservation of molecular contacts between successive tetramers mediated by the L(45) loops as seen in two other crystal forms of SSBc, suggesting a possible functional relevance of this interaction.

PubMed: 15169953
DOI: 10.1110/ps.04661904

Experimental method

X-RAY DIFFRACTION (3.3 Å)