7KKF

Crystal Structure of S. cerevisiae Ess1

Summary for 7KKF

• Entry DOI: 10.2210/pdb7kkf/pdb
• Related: 1PIN 1YW5
• Descriptor: Peptidyl-prolyl cis-trans isomerase ESS1 (2 entities in total)
• Functional Keywords: ess1, prolyl isomerase, transcription, isomerase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 38743.31

Authors

Namitz, K.E.W.,Alicea-Velazquez, N.L.,Cosgrove, M.S.,Hanes, S.D. (deposition date: 2020-10-27, release date: 2021-03-31, Last modification date: 2023-10-18)

Primary citation

Namitz, K.E.W.,Zheng, T.,Canning, A.J.,Alicea-Velazquez, N.L.,Castaneda, C.A.,Cosgrove, M.S.,Hanes, S.D.
Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.
Commun Biol, 4:398-398, 2021

PubMed Abstract: Accurate gene transcription in eukaryotes depends on isomerization of serine-proline bonds within the carboxy-terminal domain (CTD) of RNA polymerase II. Isomerization is part of the "CTD code" that regulates recruitment of proteins required for transcription and co-transcriptional RNA processing. Saccharomyces cerevisiae Ess1 and its human ortholog, Pin1, are prolyl isomerases that engage the long heptad repeat (YSPTSPS) of the CTD by an unknown mechanism. Here, we used an integrative structural approach to decipher Ess1 interactions with the CTD. Ess1 has a rigid linker between its WW and catalytic domains that enforces a distance constraint for bivalent interaction with the ends of long CTD substrates (≥4-5 heptad repeats). Our binding results suggest that the Ess1 WW domain anchors the proximal end of the CTD substrate during isomerization, and that linker divergence may underlie evolution of substrate specificity.

PubMed: 33767358
DOI: 10.1038/s42003-021-01906-8

Experimental method

X-RAY DIFFRACTION (2.4 Å)