PASTA domain

PASTA domain
Cartoon representation of PASTA domain from Staphylococcus aureus. PDB entry 3m9g
Identifiers
SymbolPASTA
PfamPF03793
InterProIPR005543
SMARTPASTA
PROSITEPDOC51178
SCOP21rp5 / SCOPe / SUPFAM
CDDcd06573
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1k25​A:694-750, 1qme​A:694-750, 1rp5​B:694-750, 1qmf​A:694-750, 1pyy​A:694-750

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.

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 (protein kinase B) 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 Bacillota and Actinomycetota.

References

  1. ^ Yeats C, Finn RD, Bateman A (September 2002). "The PASTA domain: a beta-lactam-binding domain". Trends Biochem. Sci. 27 (9): 438–440. 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.