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1vm4

From Proteopedia

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{{STRUCTURE_1vm4| PDB=1vm4 | SCENE= }}
{{STRUCTURE_1vm4| PDB=1vm4 | SCENE= }}
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'''Solution structure of an antibacterial and antitumor peptide designed based on the N-terminal membrane anchor of E. coli enzyme IIA (Glucose)'''
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===Solution structure of an antibacterial and antitumor peptide designed based on the N-terminal membrane anchor of E. coli enzyme IIA (Glucose)===
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==Overview==
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To understand the functional differences between a nontoxic membrane anchor corresponding to the N-terminal sequence of the Escherichia coli enzyme IIA(Glc) and a toxic antimicrobial peptide aurein 1.2 of similar sequence, a series of peptides was designed to bridge the gap between them. An alteration of a single residue of the membrane anchor converted it into an antibacterial peptide. Circular dichroism spectra indicate that all peptides are disordered in water but helical in micelles. Structures of the peptides were determined in membrane-mimetic micelles by solution NMR spectroscopy. The quality of the distance-based structures was improved by including backbone angle restraints derived from a set of chemical shifts ((1)H(alpha), (15)N, (13)C(alpha), and (13)C(beta)) from natural abundance two-dimensional heteronuclear correlated spectroscopy. Different from the membrane anchor, antibacterial peptides possess a broader and longer hydrophobic surface, allowing a deeper penetration into the membrane, as supported by intermolecular nuclear Overhauser effect cross-peaks between the peptide and short chain dioctanoyl phosphatidylglycerol. An attempt was made to correlate the NMR structures of these peptides with their antibacterial activity. The activity of this group of peptides does not correlate exactly with helicity, amphipathicity, charge, the number of charges, the size of the hydrophobic surface, or hydrophobic transfer free energy. However, a correlation is established between the peptide activity and membrane perturbation potential, which is defined by interfacial hydrophobic patches and basic residues in the case of cationic peptides. Indeed, (31)P solid state NMR spectroscopy of lipid bilayers showed that the extent of lipid vesicle disruption by these peptides is proportional to their membrane perturbation potential.
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(as it appears on PubMed at http://www.pubmed.gov), where 15572363 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15572363}}
==About this Structure==
==About this Structure==
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VM4 OCA].
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Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VM4 OCA].
==Reference==
==Reference==
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[[Category: Antimicrobial peptide]]
[[Category: Antimicrobial peptide]]
[[Category: Bacterial membrane anchor]]
[[Category: Bacterial membrane anchor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:42:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:12:50 2008''

Revision as of 03:12, 29 July 2008

Image:1vm4.png

Template:STRUCTURE 1vm4

Solution structure of an antibacterial and antitumor peptide designed based on the N-terminal membrane anchor of E. coli enzyme IIA (Glucose)

Template:ABSTRACT PUBMED 15572363

About this Structure

Full experimental information is available from OCA.

Reference

Correlation of three-dimensional structures with the antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor., Wang G, Li Y, Li X, J Biol Chem. 2005 Feb 18;280(7):5803-11. Epub 2004 Nov 30. PMID:15572363

Page seeded by OCA on Tue Jul 29 06:12:50 2008

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