The thumb's knuckle

Flexibility in the thumb subdomain of T7 RNA polymerase is revealed by the structure of a chimeric T7/T3 RNA polymerase

Rui J Sousa, John Rose, B. C. Wang

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

We have solved the structure of a chimeric T7/T3 RNA polymerase (RNAP) in an orthorhombic crystal by molecular replacement with the T7 RNAP structure determined from a monoclinic crystal. The structure of the protruding "thumb" subdomain of the polymerase appears very different in these two crystals apparently because of differences in packing contacts made by the thumb subdomain. These observations support the proposal that the thumb subdomain is flexible and can wrap around bound template to obstruct polymerase : template dissociation during processive synthesis.

Original languageEnglish (US)
Pages (from-to)6-12
Number of pages7
JournalJournal of Molecular Biology
Volume244
Issue number1
StatePublished - 1994

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Thumb
bacteriophage T7 RNA polymerase
bacteriophage T3 RNA polymerase

Keywords

  • Molecular replacement
  • Polymerase
  • Processivity
  • Protein flexibility
  • RNA polymerase

ASJC Scopus subject areas

  • Virology

Cite this

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AB - We have solved the structure of a chimeric T7/T3 RNA polymerase (RNAP) in an orthorhombic crystal by molecular replacement with the T7 RNAP structure determined from a monoclinic crystal. The structure of the protruding "thumb" subdomain of the polymerase appears very different in these two crystals apparently because of differences in packing contacts made by the thumb subdomain. These observations support the proposal that the thumb subdomain is flexible and can wrap around bound template to obstruct polymerase : template dissociation during processive synthesis.

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