1EF4
SOLUTION STRUCTURE OF THE ESSENTIAL RNA POLYMERASE SUBUNIT RPB10 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
1EF4 の概要
エントリーDOI | 10.2210/pdb1ef4/pdb |
分子名称 | DNA-DIRECTED RNA POLYMERASE, ZINC ION (2 entities in total) |
機能のキーワード | three helix bundle, zinc binding, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, transferase |
由来する生物種 | Methanothermobacter thermautotrophicus |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 6509.90 |
構造登録者 | Mackereth, C.D.,Arrowsmith, C.H.,Edwards, A.M.,Mcintosh, L.P.,Northeast Structural Genomics Consortium (NESG) (登録日: 2000-02-07, 公開日: 2000-06-14, 最終更新日: 2024-05-22) |
主引用文献 | Mackereth, C.D.,Arrowsmith, C.H.,Edwards, A.M.,McIntosh, L.P. Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum. Proc.Natl.Acad.Sci.USA, 97:6316-6321, 2000 Cited by PubMed Abstract: The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast. Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a zinc-bundle, consisting of three alpha-helices stabilized by a zinc ion. The metal ion is bound within an atypical CX(2)CX(n)CC sequence motif and serves to bridge an N-terminal loop with helix 3. This represents an example of two adjacent zinc-binding Cys residues within an alpha-helix conformation. Conserved surface features of RPB10 include discrete regions of neutral, acidic, and basic residues, the latter being located around the zinc-binding site. One or more of these regions may contribute to the role of this subunit as a scaffold protein within the polymerase holoenzyme. PubMed: 10841539DOI: 10.1073/pnas.97.12.6316 主引用文献が同じPDBエントリー |
実験手法 | SOLUTION NMR |
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