PASTA domain

The PASTA domain is a small protein domain that can bind to the beta-lactam ring portion of various β-lactam 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.

PASTA domain
Cartoon representation of PASTA domain from Staphylococcus aureus. PDB entry 3m9g
Identifiers
SymbolPASTA
PfamPF03793
InterProIPR005543
SMARTPASTA
PROSITEPDOC51178
SCOPe1rp5 / SUPFAM
CDDcd06573

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.

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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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