1EF4

SOLUTION STRUCTURE OF THE ESSENTIAL RNA POLYMERASE SUBUNIT RPB10 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

Summary for 1EF4

• Entry DOI: 10.2210/pdb1ef4/pdb
• Descriptor: DNA-DIRECTED RNA POLYMERASE, ZINC ION (2 entities in total)
• Functional Keywords: three helix bundle, zinc binding, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, transferase
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 1
• Total formula weight: 6509.90

Authors

Mackereth, C.D.,Arrowsmith, C.H.,Edwards, A.M.,Mcintosh, L.P.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2000-02-07, release date: 2000-06-14, Last modification date: 2024-05-22)

Primary citation

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

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: 10841539
DOI: 10.1073/pnas.97.12.6316

Experimental method

SOLUTION NMR