โ Scribed by L. Whitmore; J. K. Chugh; C. F. Snook; Dr B. A. Wallace
No coin nor oath required. For personal study only.
The peptaibols are a large family of membraneโactive peptides with considerable sequence homology, but with different biological properties and threeโdimensional structures. They constitute a rich resource of naturally occurring โmutantsโ which are potentially valuable for structure/function studies of ion channels.
A searchable onโline database of sequences and structures of the peptaibols has been created at http://www.cryst.bbk.ac.uk/peptaibol, as a resource for the biological and structural community. In this paper, the contents and organization of the website are discussed as well as procedures for submission of new entries to the database.
At present, more than 300 peptaibol sequences are stored in the database. Each sequence entry contains its full literature reference and information about its biological source. Tools are provided for searching for specific peptaibol sequences or groupings of sequences, and for locating peptaibols containing specified sequence motifs. In addition the website acts as a database for structural information. The coordinates of all currently available peptaibol xโray and NMR structures are included and complemented, where appropriate, with molecular graphics illustrations. These include figures of model channel structures and comparisons between different peptaibol structures. The peptaibol database thus provides a tool for ready access to information and a means of investigating the sequences and structures of this class of polypeptides. Copyright ยฉ 2003 European Peptide Society and John Wiley & Sons, Ltd.
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Communicated by David N
From the culture broth of the mold Trichoderma viride, strain 63 C-I, the polypeptide antibiotic suzukacillin (SZ) was isolated. A peptide mixture named SZ-A was obtained by crystallization from crude SZ. Individual peptides from SZ-A were isolated by semipreparative HPLC and sequences were determin