3CB6
Crystal Structure of the S. pombe Peptidase Homology Domain of FACT complex subunit Spt16 (form B)
Summary for 3CB6
| Entry DOI | 10.2210/pdb3cb6/pdb |
| Related | 3BIP 3BIQ 3BIT 3CB5 |
| Descriptor | FACT complex subunit spt16 (2 entities in total) |
| Functional Keywords | peptidase homology domain, histone binding module, histone h3/h4 chaperone, pita-bread fold, chromosomal protein, dna damage, dna repair, dna replication, nucleus, transcription, transcription regulation |
| Biological source | Schizosaccharomyces pombe (Fission yeast) |
| Cellular location | Nucleus (By similarity): O94267 |
| Total number of polymer chains | 1 |
| Total formula weight | 49987.77 |
| Authors | Stuwe, T.,Hothorn, M.,Lejeune, E.,Bortfeld-Miller, M.,Scheffzek, K.,Ladurner, A.G. (deposition date: 2008-02-21, release date: 2008-06-17, Last modification date: 2023-11-01) |
| Primary citation | Stuwe, T.,Hothorn, M.,Lejeune, E.,Rybin, V.,Bortfeld, M.,Scheffzek, K.,Ladurner, A.G. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module Proc.Natl.Acad.Sci.USA, 105:8884-8889, 2008 Cited by PubMed Abstract: The FACT complex is a conserved cofactor for RNA polymerase II elongation through nucleosomes. FACT bears histone chaperone activity and contributes to chromatin integrity. However, the molecular mechanisms behind FACT function remain elusive. Here we report biochemical, structural, and mutational analyses that identify the peptidase homology domain of the Schizosaccharomyces pombe FACT large subunit Spt16 (Spt16-N) as a binding module for histones H3 and H4. The 2.1-A crystal structure of Spt16-N reveals an aminopeptidase P fold whose enzymatic activity has been lost. Instead, the highly conserved fold directly binds histones H3-H4 through a tight interaction with their globular core domains, as well as with their N-terminal tails. Mutations within a conserved surface pocket in Spt16-N or posttranslational modification of the histone H4 tail reduce interaction in vitro, whereas the globular domains of H3-H4 and the H3 tail bind distinct Spt16-N surfaces. Our analysis suggests that the N-terminal domain of Spt16 may add to the known H2A-H2B chaperone activity of FACT by including a H3-H4 tail and H3-H4 core binding function mediated by the N terminus of Spt16. We suggest that these interactions may aid FACT-mediated nucleosome reorganization events. PubMed: 18579787DOI: 10.1073/pnas.0712293105 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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