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4RW5

Structural insights into substrate binding of brown spider venom class II phospholipases D

Summary for 4RW5
Entry DOI10.2210/pdb4rw5/pdb
Related4RW3
DescriptorPhospholipase D LiSicTox-alphaIA1bii, MAGNESIUM ION, PALMITIC ACID, ... (7 entities in total)
Functional Keywordstim-barrel fold, hydrolase
Biological sourceLoxosceles intermedia (Brown spider)
Cellular locationSecreted : P0CE82
Total number of polymer chains1
Total formula weight34404.00
Authors
Coronado, M.A.,Ullah, A.,da Silva, L.S.,Chaves-Moreira, D.,Vuitika, L.,Chaim, O.M.,Veiga, S.S.,Chahine, J.,Murakami, M.T.,Arni, R.K. (deposition date: 2014-12-01, release date: 2015-06-03, Last modification date: 2024-11-06)
Primary citationCoronado, M.A.,Ullah, A.,da Silva, L.S.,Chaves-Moreira, D.,Vuitika, L.,Chaim, O.M.,Veiga, S.S.,Chahine, J.,Murakami, M.T.,Arni, R.K.
Structural Insights into Substrate Binding of Brown Spider Venom Class II Phospholipases D.
Curr Protein Pept Sci, 16:768-774, 2015
Cited by
PubMed Abstract: Phospholipases D (PLDs), the major dermonecrotic factors from brown spider venoms, trigger a range of biological reactions both in vitro and in vivo. Despite their clinical relevance in loxoscelism, structural data is restricted to the apo-form of these enzymes, which has been instrumental in understanding the functional differences between the class I and II spider PLDs. The crystal structures of the native class II PLD from Loxosceles intermedia complexed with myo-inositol 1-phosphate and the inactive mutant H12A complexed with fatty acids indicate the existence of a strong ligand-dependent conformation change of the highly conserved aromatic residues, Tyr 223 and Trp225 indicating their roles in substrate binding. These results provided insights into the structural determinants for substrate recognition and binding by class II PLDs.
PubMed: 25961401
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.64 Å)
Structure validation

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