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2CKZ

X-ray structure of RNA polymerase III subcomplex C17-C25.

Summary for 2CKZ
Entry DOI10.2210/pdb2ckz/pdb
DescriptorDNA-DIRECTED RNA POLYMERASE III 18 KD POLYPEPTIDE, DNA-DIRECTED RNA POLYMERASE III 25 KD POLYPEPTIDE (2 entities in total)
Functional Keywordsdna-directed rna polymerase, multiprotein complex, nucleotidyltransferase, nuclear protein, hypothetical protein, eukaryotic nucleic acid polymerase, class iii gene transcription, transferase, transcription, trna synthesis
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
More
Cellular locationNucleus : P47076
Total number of polymer chains4
Total formula weight87631.60
Authors
Jasiak, A.J.,Armache, K.-J.,Martens, B.,Jansen, R.-P.,Cramer, P. (deposition date: 2006-04-24, release date: 2006-07-13, Last modification date: 2024-05-08)
Primary citationJasiak, A.J.,Armache, K.-J.,Martens, B.,Jansen, R.-P.,Cramer, P.
Structural Biology of RNA Polymerase III: Subcomplex C17/-C25 X-Ray Structure and 11-Subunit Enzyme Model
Mol.Cell, 23:71-, 2006
Cited by
PubMed Abstract: We obtained an 11 subunit model of RNA polymerase (Pol) III by combining a homology model of the nine subunit core enzyme with a new X-ray structure of the subcomplex C17/25. Compared to Pol II, Pol III shows a conserved active center for RNA synthesis but a structurally different upstream face for specific initiation complex assembly during promoter selection. The Pol III upstream face includes a HRDC domain in subunit C17 that is translated by 35 A and rotated by 150 degrees compared to its Pol II counterpart. The HRDC domain is essential in vivo, folds independently in vitro, and, unlike other HRDC domains, shows no indication of nucleic acid binding. Thus, the HRDC domain is a functional module that could account for the role of C17 in Pol III promoter-specific initiation. During elongation, C17/25 may bind Pol III transcripts emerging from the adjacent exit pore, because the subcomplex binds to tRNA in vitro.
PubMed: 16818233
DOI: 10.1016/J.MOLCEL.2006.05.013
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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