3HKZ

The X-ray crystal structure of RNA polymerase from Archaea

3HKZ の概要

• エントリーDOI: 10.2210/pdb3hkz/pdb
• 関連するPDBエントリー: 2PA8 2WAQ 2pmz
• 分子名称: DNA-directed RNA polymerase subunit A', DNA-directed RNA polymerase subunit L, DNA-directed RNA polymerase subunit N, ... (16 entities in total)
• 機能のキーワード: rna polymerase, archaea, sulfolobus solfataricus, dna-directed rna polymerase, metal-binding, nucleotidyltransferase, transcription, transferase, zinc, zinc-finger
• 由来する生物種: Sulfolobus solfataricus; 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 811622.29

構造登録者

Murakami, K.S. (登録日: 2009-05-26, 公開日: 2009-06-09, 最終更新日: 2024-11-06)

主引用文献

Hirata, A.,Klein, B.J.,Murakami, K.S.
The X-ray crystal structure of RNA polymerase from Archaea.
Nature, 451:851-854, 2008

PubMed Abstract: The transcription apparatus in Archaea can be described as a simplified version of its eukaryotic RNA polymerase (RNAP) II counterpart, comprising an RNAPII-like enzyme as well as two general transcription factors, the TATA-binding protein (TBP) and the eukaryotic TFIIB orthologue TFB. It has been widely understood that precise comparisons of cellular RNAP crystal structures could reveal structural elements common to all enzymes and that these insights would be useful in analysing components of each enzyme that enable it to perform domain-specific gene expression. However, the structure of archaeal RNAP has been limited to individual subunits. Here we report the first crystal structure of the archaeal RNAP from Sulfolobus solfataricus at 3.4 A resolution, completing the suite of multi-subunit RNAP structures from all three domains of life. We also report the high-resolution (at 1.76 A) crystal structure of the D/L subcomplex of archaeal RNAP and provide the first experimental evidence of any RNAP possessing an iron-sulphur (Fe-S) cluster, which may play a structural role in a key subunit of RNAP assembly. The striking structural similarity between archaeal RNAP and eukaryotic RNAPII highlights the simpler archaeal RNAP as an ideal model system for dissecting the molecular basis of eukaryotic transcription.

PubMed: 18235446
DOI: 10.1038/nature06530

実験手法

X-RAY DIFFRACTION (3.4 Å)