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2KYA

Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34

Summary for 2KYA
Entry DOI10.2210/pdb2kya/pdb
NMR InformationBMRB: 16943
DescriptorPatellamide protein (1 entity in total)
Functional Keywordscyclic peptides, pate, patellamides, prochloron, ribosomal peptide synthetase, unknown function
Biological sourceProchloron didemni
Total number of polymer chains1
Total formula weight3709.25
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 citationHoussen, 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: 20715266
DOI: 10.1002/cbic.201000305
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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