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2JR3

Antibacterial Peptide from Eggshell Matrix: Structure and Self-assembly of beta-defensin Like Peptide from the Chinese Soft-shelled Turtle Eggshell

Summary for 2JR3
Entry DOI10.2210/pdb2jr3/pdb
NMR InformationBMRB: 15318
DescriptorPelovaterin (1 entity in total)
Functional Keywordsbeta-defensin like peptide, chinese soft-shelled turtle eggshell, antibacterial peptide, eggshell matrix, antimicrobial protein
Biological sourcePelodiscus sinensis (Chinese softshell turtle)
Total number of polymer chains1
Total formula weight4198.85
Authors
Vivekanandan, S.,Lakshminarayanan, R.,Jois, S.D.S.,Perumal Samy, R.,Banerjee, Y.,Chi-Jin, E.O.,Teo, K.W.,Kini, R.M.,Valiyaveettil, S. (deposition date: 2007-06-20, release date: 2008-05-27, Last modification date: 2024-11-06)
Primary citationLakshminarayanan, R.,Vivekanandan, S.,Samy, R.P.,Banerjee, Y.,Chi-Jin, E.O.,Teo, K.W.,Jois, S.D.,Kini, R.M.,Valiyaveettil, S.
Structure, self-assembly, and dual role of a beta-defensin-like peptide from the Chinese soft-shelled turtle eggshell matrix.
J.Am.Chem.Soc., 130:4660-4668, 2008
Cited by
PubMed Abstract: Biomineral matrix formation and molecular recognition are two important processes associated with eggshell biomineralization. To understand these two processes, a major intracrystalline peptide, pelovaterin, was isolated from turtle (Pelodiscus sinensis) eggshell and its tertiary and quaternary structures were established. The global fold of pelovaterin is similar to that of human beta-defensins but has a large hydrophobic core and a short hydrophilic N-terminal segment, which is not preserved in defensins. Pelovaterin exhibits strong antimicrobial activity against two pathogenic gram-negative bacteria, Pseudomonas aeruginosa and Proteus vulgaris, and stabilizes a thin film of metastable vaterite. We show that pelovaterin self-aggregates in the form of micellar nanospheres and the aggregation in solution is entropy-driven. It is suggested that the micellar aggregation of pelovaterin is responsible for the induction and stabilization of the metastable phase by altering the interfacial energy. The results demonstrate the adaptability of an extracellular matrix protein to perform multiple tasks: polymorph discrimination and protection of the contents of the egg against bacterial invasion.
PubMed: 18341335
DOI: 10.1021/ja075659k
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-06-18公开中

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