6my1

Solution structure of gomesin at 278 K

spinqualitylabelsall models 6my1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6my1 is a 1 chain structure with sequence from Acanthoscurria gomesiana. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Ligands: NH2, PCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GOME_ACAGO Active against several Gram-positive bacteria such as Bacillus spp, Staphylococcus spp and E.faecalis, several Gram-negative bacteria such as E.coli, K.pneumoniae, P.aeruginosa and Salmonella spp, filamentous fungi such as N.crassa, T.viridae and yeasts such as C.albicans. It is active against the parasite L.amazonensis as well. It shows hemolytic activity. Publication Abstract from PubMed The cross-strand disulfides (CSDs) found in beta-hairpin antimicrobial peptides (beta-AMPs) show a unique disulfide geometry that is characterized by unusual torsion angles and a short Calpha-Calpha distance. While the sequence and disulfide bond connectivity of disulfide-rich peptides is well studied, much less is known about the disulfide geometry found in CSDs and their role in the stability of beta-AMPs. To address this, we solved the nuclear magnetic resonance (NMR) structure of the beta-AMP gomesin (Gm) at 278, 298, and 310 K, examined the disulfide bond geometry of over 800 disulfide-rich peptides, and carried out extensive molecular dynamics (MD) simulation of the peptides Gm and protegrin. The NMR data suggests Calpha-Calpha distances characteristic for CSDs are independent of temperature. Analysis of disulfide-rich peptides from the Protein Data Bank revealed that right-handed and left-handed rotamers are equally likely in CSDs. The previously reported preference for right-handed rotamers was likely biased by restricting the analysis to peptides and proteins solved using X-ray crystallography. Furthermore, data from MD simulations showed that the short Calpha-Calpha distance is critical for the stability of these peptides. The unique disulfide geometry of CSDs poses a challenge to biomolecular force fields and to retain the stability of beta-hairpin fold over long simulation times, restraints on the torsion angles might be required. The unusual conformation of cross-strand disulfide bonds is critical to the stability of beta-hairpin peptides.,Deplazes E, Chin YK, King GF, Mancera RL Proteins. 2019 Oct 7. doi: 10.1002/prot.25828. PMID:31589791 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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