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Crystal structure of full length E. coli SSB proteinCrystal structure of full length E. coli SSB protein
Structural highlights
Function[SSB_ECOLI] This protein is essential for replication of the chromosomes and its single-stranded DNA phages. It is also involved in DNA recombination and repair. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA.,Savvides SN, Raghunathan S, Futterer K, Kozlov AG, Lohman TM, Waksman G Protein Sci. 2004 Jul;13(7):1942-7. Epub 2004 May 28. PMID:15169953[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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