3GXW

Structure of the SH2 domain of the Candida glabrata transcription elongation factor Spt6, crystal form A

Summary for 3GXW

• Entry DOI: 10.2210/pdb3gxw/pdb
• Related: 3GXX
• Descriptor: Transcription elongation factor SPT6, SUCCINIC ACID, SODIUM ION, ... (4 entities in total)
• Functional Keywords: sh2-fold, three stranded anti-parallel beta sheet, n-terminal alpha helix, c-terminal alpha helix, nucleus, sh2 domain, transcription, transcription regulation
• Biological source: Candida glabrata (Yeast)
• Cellular location: Nucleus (By similarity): Q6FLB1
• Total number of polymer chains: 4
• Total formula weight: 50034.43

Authors

Dengl, S.,Mayer, A.,Sun, M.,Cramer, P. (deposition date: 2009-04-03, release date: 2009-05-26, Last modification date: 2024-11-06)

Primary citation

Dengl, S.,Mayer, A.,Sun, M.,Cramer, P.
Structure and in vivo requirement of the yeast Spt6 SH2 domain
J.Mol.Biol., 389:211-225, 2009

PubMed Abstract: During transcription elongation through chromatin, the Ser2-phosphorylated C-terminal repeat domain of RNA polymerase II binds the C-terminal Src homology 2 (SH2) domain of the nucleosome re-assembly factor Spt6. This SH2 domain is unusual in its specificity to bind phosphoserine, rather than phosphotyrosine and because it is the only SH2 domain in the yeast genome. Here, we report the high-resolution crystal structure of the SH2 domain from Candida glabrata Spt6. The structure combines features from both structural subfamilies of SH2 domains, suggesting it resembles a common ancestor of all SH2 domains. Two conserved surface pockets deviate from those of canonical SH2 domains, and may explain the unusual phosphoserine specificity. Differential gene expression analysis reveals that the SH2 domain is required for normal expression of a subset of yeast genes, and is consistent with multiple functions of Spt6 in chromatin transcription.

PubMed: 19371747
DOI: 10.1016/j.jmb.2009.04.016

Experimental method

X-RAY DIFFRACTION (1.9 Å)