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PDBsum entry 1dqc

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Antimicrobial protein PDB id
1dqc
Contents
Protein chain
74 a.a. *
* Residue conservation analysis

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Key reference
Title Chitin-Binding proteins in invertebrates and plants comprise a common chitin-Binding structural motif.
Authors T.Suetake, S.Tsuda, S.Kawabata, K.Miura, S.Iwanaga, K.Hikichi, K.Nitta, K.Kawano.
Ref. J Biol Chem, 2000, 275, 17929-17932. [DOI no: 10.1074/jbc.C000184200]
PubMed id 10770921
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.
Figure 1.
Fig. 1. Solution structure of tachycitin. A, stereo view of the best-fit superposition of 25 structures of tachycitin using backbone atoms (C^ , C, and N) of residues 6-68. B, ribbon representation of the minimized average structure of tachycitin. Disulfide bonds (yellow), -sheets (blue), and an helical turn (red) are indicated. Drawings were prepared using MOLMOL (26).
Figure 3.
Fig. 3. Putative chitin-binding site of tachycitin (Cys-40-Gly-60) superimposed onto the previously identified chitin-binding site of hevein (Cys-12-Ser-32). The conserved disulfide bonds are colored in green. Residues of Asn-47, Tyr-49, and Val-52 in the -hairpin of tachycitin (red) are superimposed onto the chitin-binding residues of hevein (blue).
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2000, 275, 17929-17932) copyright 2000.
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