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Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing | Academic Article individual record
abstract

Several genes from prokaryotes and lower eukaryotes have been found to contain an in-frame open reading frame, which encodes for an internal protein (intein). Post-translationally, the internal polypeptide auto-splices and ligates the external sequences to yield a functional external protein (extein) and an intein. Most, but not all inteins, contain, apart from a splicing domain, a separate endonucleolytic domain that enables them to maintain their presence by a homing mechanism. We report here the crystal structure of an intein found in the gyrase A subunit from Mycobacterium xenopi at 2.2 A resolution. The structure contains an unusual beta-fold with the catalytic splice junctions at the ends of two adjacent antiparallel beta-strands. The arrangement of the active site residues Ser 1, Thr 72, His 75, His 197, and Asn 198 is consistent with a four-step mechanism for the cleavage-ligation reaction. Using site-directed mutagenesis, the N-terminal cysteine, proposed as the nucleophile in the first step of the splicing reaction, was changed to a Ser 1 and Ala 0, thus capturing the intein in a pre-spliced state.

author list (cited authors)
Klabunde, T., Sharma, S., Telenti, A., Jacobs, W. R., & Sacchettini, J. C.
publication date
1998
keywords
  • Saccharomyces Cerevisiae Proteins
  • Insect Proteins
  • Dna Gyrase
  • Endonucleases
  • Mycobacterium Xenopi
  • Drosophila Proteins
  • Amino Acid Sequence
  • Dna Topoisomerases, Type Ii
  • Protein Splicing
  • Protein Structure, Tertiary
  • Deoxyribonucleases, Type II Site-Specific
  • Molecular Sequence Data
  • Protein Precursors
  • Saccharomyces Cerevisiae
  • Hedgehog Proteins
altmetric score

3.0

citation count

190