2KYA
Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34
Summary for 2KYA
Entry DOI | 10.2210/pdb2kya/pdb |
NMR Information | BMRB: 16943 |
Descriptor | Patellamide protein (1 entity in total) |
Functional Keywords | cyclic peptides, pate, patellamides, prochloron, ribosomal peptide synthetase, unknown function |
Biological source | Prochloron didemni |
Total number of polymer chains | 1 |
Total formula weight | 3709.25 |
Authors | Houssen, W.E.,Wright, S.H.,Kalverda, A.P.,Thompson, G.S.,Kelly, S.M.,Jaspars, M. (deposition date: 2010-05-21, release date: 2010-09-01, Last modification date: 2024-05-01) |
Primary citation | Houssen, W.E.,Wright, S.H.,Kalverda, A.P.,Thompson, G.S.,Kelly, S.M.,Jaspars, M. Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE(1-34). Chembiochem, 11:1867-1873, 2010 Cited by PubMed Abstract: The solution structure of the leader sequence of the patellamide precursor peptide was analysed by using CD and determined with NOE-restrained molecular dynamics calculations. This leader sequence is highly conserved in the precursor peptides of some other cyanobactins harbouring heterocycles, and is assumed to play a role in targeting the precursor peptide to the post-translational machinery. The sequence was observed to form an alpha-helix spanning residues 13-28 with a hydrophobic surface on one side of the helix. This hydrophobic surface is proposed to be the site of the initial binding with modifying enzymes. PubMed: 20715266DOI: 10.1002/cbic.201000305 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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