1DQC

SOLUTION STRUCTURE OF TACHYCITIN, AN ANTIMICROBIAL PROTEIN WITH CHITIN-BINDING FUNCTION

Summary for 1DQC

• Entry DOI: 10.2210/pdb1dqc/pdb
• Descriptor: TACHYCITIN (1 entity in total)
• Functional Keywords: disulfide-rich, antimicrobial protein
• Biological source: Tachypleus tridentatus
• Total number of polymer chains: 1
• Total formula weight: 8383.70

Authors

Suetake, T.,Tsuda, S.,Kawabata, S.,Miura, K.,Kawano, K. (deposition date: 2000-01-04, release date: 2000-09-13, Last modification date: 2024-11-06)

Primary citation

Suetake, T.,Tsuda, S.,Kawabata, S.,Miura, K.,Iwanaga, S.,Hikichi, K.,Nitta, K.,Kawano, K.
Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif.
J.Biol.Chem., 275:17929-17932, 2000

PubMed Abstract: Tachycitin, a 73-residue polypeptide having antimicrobial activity is present in the hemocyte of horseshoe crab (Tachypleus tridentatus). The first three-dimensional structure of invertebrate chitin-binding protein was determined for tachycitin using two-dimensional nuclear magnetic resonance spectroscopy. The measurements indicate that the structure of tachycitin is largely divided into N- and C-terminal domains; the former comprises a three-stranded beta-sheet and the latter a two-stranded beta-sheet following a short helical turn. The latter structural motif shares a significant tertiary structural similarity with the chitin-binding domain of plant chitin-binding protein. This result is thought to provide faithful experimental evidence to the recent hypothesis that chitin-binding proteins of invertebrates and plants are correlated by a convergent evolution process.

PubMed: 10770921
DOI: 10.1074/jbc.C000184200

Experimental method

SOLUTION NMR