PASTA domain

PASTA domain

Structure the PASTA domain in a penicillin binding protein.
Identifiers
Symbol PASTA
Pfam PF03793
InterPro IPR005543
SMART PASTA
PROSITE PDOC51178
SCOP 1rp5
SUPERFAMILY 1rp5
CDD cd06573

The PASTA domain is a small protein domain that can bind to beta-lactam rings found in antibiotics.[1] The domain was initially discovered in 2002 by Yeats and colleagues as a region of sequence similarity found in penicillin binding proteins and PknB-like kinases found in some bacteria. The name is an acronym derived from PBP and Serine/Threonine kinase Associated domain.

Structure

The PASTA domain adopts a structure composed of an alpha-helix followed by three beta strands. Recent structural studies show that the extracellular region of PknB that is composed of four PASTA domains shows a linear arrangement of the domains.[2]

Species distribution

PASTA domains are found in a variety of bacterial species including gram-positive firmicutes and actinobacteria.

References

  1. Yeats C, Finn RD, Bateman A (September 2002). "The PASTA domain: a beta-lactam-binding domain". Trends Biochem. Sci. 27 (9): 438. doi:10.1016/s0968-0004(02)02164-3. PMID 12217513.
  2. Barthe P, Mukamolova GV, Roumestand C, Cohen-Gonsaud M (May 2010). "The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation". Structure 18 (5): 606–15. doi:10.1016/j.str.2010.02.013. PMID 20462494.
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