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1cw5

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{{STRUCTURE_1cw5| PDB=1cw5 | SCENE= }}
{{STRUCTURE_1cw5| PDB=1cw5 | SCENE= }}
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'''SOLUTION STRUCTURE OF CARNOBACTERIOCIN B2'''
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===SOLUTION STRUCTURE OF CARNOBACTERIOCIN B2===
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==Overview==
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Carnobacteriocin B2 (CbnB2), a type IIa bacteriocin, is a 48 residue antimicrobial peptide from the lactic acid bacterium Carnobacterium pisicola LV17B. Type IIa bacteriocins have a conserved YGNGVXC sequence near the N-terminus and usually contain a disulfide bridge. CbnB2 seemed to be unique in that its two cysteines (Cys9 and Cys14) could be isolated as free thiols [Quadri et al. (1994) J. Biol. Chem. 26, 12204-12211]. To establish the structural consequences of the presence or absence of a disulfide bridge and to investigate if the YGNGVXC sequence is a receptor-binding motif [Fleury et al. (1996) J. Biol. Chem. 271, 14421-14429], the three-dimensional solution structure of CbnB2 was determined by two-dimensional (1)H nuclear magnetic resonance (NMR) techniques. Mass spectroscopic and thiol modification experiments on CbnB2 and on model peptides, in conjunction with activity measurements, were used to verify the redox status of CbnB2. The results show that CbnB2 readily forms a disulfide bond and that this peptide has full antimicrobial activity. NMR results indicate that CbnB2 in trifluoroethanol (TFE) has a well-defined central helical structure (residues 18-39) but a disordered N terminus. Comparison of the CbnB2 structure with the refined solution structure of leucocin A (LeuA), another type IIa bacteriocin, indicates that the central helical structure is conserved between the two peptides despite differences in sequence but that the N-terminal structure (a proposed receptor binding site) is not. This is unexpected because LeuA and CbnB2 exhibit &gt;66% sequence identity in the first 24 residues. This suggests that the N-terminus, which had been proposed [Fleury et al. (1996) J. Biol. Chem. 271, 14421-14429] to be a receptor binding site of type IIa bacteriocins, may not be directly involved and that recognition of the amphiphilic helical portion is the critical feature.
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{{ABSTRACT_PUBMED_10569926}}
==About this Structure==
==About this Structure==
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1CW5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Carnobacterium_maltaromaticum Carnobacterium maltaromaticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CW5 OCA].
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1CW5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Carnobacterium_maltaromaticum Carnobacterium maltaromaticum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CW5 OCA].
==Reference==
==Reference==
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[[Category: Bacteriocin]]
[[Category: Bacteriocin]]
[[Category: Helix]]
[[Category: Helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:10:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:35:51 2008''

Revision as of 18:35, 30 June 2008

Image:1cw5.png

Template:STRUCTURE 1cw5

SOLUTION STRUCTURE OF CARNOBACTERIOCIN B2

Template:ABSTRACT PUBMED 10569926

About this Structure

1CW5 is a Single protein structure of sequence from Carnobacterium maltaromaticum. Full experimental information is available from OCA.

Reference

Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria., Wang Y, Henz ME, Gallagher NL, Chai S, Gibbs AC, Yan LZ, Stiles ME, Wishart DS, Vederas JC, Biochemistry. 1999 Nov 23;38(47):15438-47. PMID:10569926

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