5emx

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Crystal structure of the S. cerevisiae Rtf1 histone modification domain mutant R124A R126A R128ACrystal structure of the S. cerevisiae Rtf1 histone modification domain mutant R124A R126A R128A

Structural highlights

5emx is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.399Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RTF1_YEAST The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. Important for TATA site selection by TBP. Directly or indirectly regulates the DNA-binding properties of SPT15, the TATA box-binding protein, and the relative activities of different TATA elements.[1] [2]

References

  1. Porter SE, Penheiter KL, Jaehning JA. Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization. Eukaryot Cell. 2005 Jan;4(1):209-20. PMID:15643076 doi:http://dx.doi.org/10.1128/EC.4.1.209-220.2005
  2. Sheldon KE, Mauger DM, Arndt KM. A Requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation. Mol Cell. 2005 Oct 28;20(2):225-36. PMID:16246725 doi:S1097-2765(05)01568-6

5emx, resolution 1.40Å

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OCA