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PASTA domain

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This is an old revision of this page, as edited by DMacks (talk | contribs) at 18:01, 21 October 2019 (top: grammar cleanup...sentence could have implied that the PASTA domain was part of the antibiotic). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

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 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.