Structure of Antimicrobial Peptide, HP (2-20) and its Analogues Derived from Helicobacter pylori, as Determined by 1H NMR SpectroscopyStructure of Antimicrobial Peptide, HP (2-20) and its Analogues Derived from Helicobacter pylori, as Determined by 1H NMR Spectroscopy

Structural highlights

1ot0 is a 1 chain structure with sequence from Helicobacter pylori. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL1_HELPY Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity).[HAMAP-Rule:MF_01318] Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA (By similarity).[HAMAP-Rule:MF_01318] Peptides originating from the N-terminal end of L1 have antibacterial activity against bacteria such as E.coli and B.megaterium and modest antifungal activities. Has no effect on H.pylori itself. Peptides are not hemolytic against mammalian cells. These peptides may be released in the stomach during altruistic lysis to kill other fast growing bacteria.[HAMAP-Rule:MF_01318]

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