2leu: Difference between revisions

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[[Image:2leu.jpg|left|200px]]<br /><applet load="2leu" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2leu.jpg|left|200px]]<br /><applet load="2leu" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2leu" />

'''HIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN 90% AQUEOUS TRIFLUOROETHANOL (TFE) (0.1% TFA), 18 STRUCTURES'''<br />

==Overview==

The first three-dimensional structure of a type IIa bacteriocin from, lactic acid bacteria is reported. Complete 1H resonance assignments of, leucocin A, a 37 amino acid antimicrobial peptide isolated from the lactic, acid bacterium Leuconostoc gelidum UAL187, were determined in 90%, trifluoroethanol (TFE)-water and in aqueous dodecylphosphocholine (DPC), micelles (1:40 ratio of leucocin A:DPC) using two-dimensional NMR, techniques (e.g., DQF-COSY, TOCSY, NOESY). Circular dichroism spectra, NMR, chemical shift indices, amide hydrogen exchange rates, and long-range, nuclear Overhauser effects indicate that leucocin A adopts a reasonably, well defined structure in both TFE and DPC micelle environments but exists, as a random coil in water or aqueous DMSO. Distance geometry and simulated, annealing calculations were employed to generate structures for leucocin A, in both lipophilic media. While some differences were noted between the, structures calculated for the two different solvent systems, in both, the, region encompassing residues 17-31 assumes an essentially identical, amphiphilic alpha-helix conformation. A three-strand antiparallel, beta-sheet domain (residues 2-16), anchored by the disulfide bridge, is, also observed in both media. In TFE, these two regions have a more defined, relationship relative to each other, while, in DPC micelles, the, C-terminus is folded back onto the alpha-helix. The implications of these, structural features with regard to the antimicrobial mechanism of action, and target recognition are discussed.

The first three-dimensional structure of a type IIa bacteriocin from lactic acid bacteria is reported. Complete 1H resonance assignments of leucocin A, a 37 amino acid antimicrobial peptide isolated from the lactic acid bacterium Leuconostoc gelidum UAL187, were determined in 90% trifluoroethanol (TFE)-water and in aqueous dodecylphosphocholine (DPC) micelles (1:40 ratio of leucocin A:DPC) using two-dimensional NMR techniques (e.g., DQF-COSY, TOCSY, NOESY). Circular dichroism spectra, NMR chemical shift indices, amide hydrogen exchange rates, and long-range nuclear Overhauser effects indicate that leucocin A adopts a reasonably well defined structure in both TFE and DPC micelle environments but exists as a random coil in water or aqueous DMSO. Distance geometry and simulated annealing calculations were employed to generate structures for leucocin A in both lipophilic media. While some differences were noted between the structures calculated for the two different solvent systems, in both, the region encompassing residues 17-31 assumes an essentially identical amphiphilic alpha-helix conformation. A three-strand antiparallel beta-sheet domain (residues 2-16), anchored by the disulfide bridge, is also observed in both media. In TFE, these two regions have a more defined relationship relative to each other, while, in DPC micelles, the C-terminus is folded back onto the alpha-helix. The implications of these structural features with regard to the antimicrobial mechanism of action and target recognition are discussed.

==About this Structure==

2LEU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leuconostoc_gelidum Leuconostoc gelidum]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2LEU OCA].

2LEU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leuconostoc_gelidum Leuconostoc gelidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEU OCA].

==Reference==

Line 13:

[[Category: Leuconostoc gelidum]]

[[Category: Single protein]]

[[Category: Gallagher, N.L.F.]]

[[Category: Gallagher, N L.F.]]

[[Category: Nakashima, T.T.]]

[[Category: Nakashima, T T.]]

[[Category: Niemczura, W.P.]]

[[Category: Niemczura, W P.]]

[[Category: Sailer, M.]]

[[Category: Stiles, M.E.]]

[[Category: Stiles, M E.]]

[[Category: Vederas, J.C.]]

[[Category: Vederas, J C.]]

[[Category: antibacterial peptide]]

[[Category: bacteriocin]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:05 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2leu.jpg|left|200px]]<br /><applet load="2leu" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2leu.jpg|left|200px]]<br /><applet load="2leu" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2leu" />
 '''HIGH RESOLUTION 1H NMR STUDY OF LEUCOCIN A IN 90% AQUEOUS TRIFLUOROETHANOL (TFE) (0.1% TFA), 18 STRUCTURES'''<br />
 ==Overview==
-The first three-dimensional structure of a type IIa bacteriocin from, lactic acid bacteria is reported. Complete 1H resonance assignments of, leucocin A, a 37 amino acid antimicrobial peptide isolated from the lactic, acid bacterium Leuconostoc gelidum UAL187, were determined in 90%, trifluoroethanol (TFE)-water and in aqueous dodecylphosphocholine (DPC), micelles (1:40 ratio of leucocin A:DPC) using two-dimensional NMR, techniques (e.g., DQF-COSY, TOCSY, NOESY). Circular dichroism spectra, NMR, chemical shift indices, amide hydrogen exchange rates, and long-range, nuclear Overhauser effects indicate that leucocin A adopts a reasonably, well defined structure in both TFE and DPC micelle environments but exists, as a random coil in water or aqueous DMSO. Distance geometry and simulated, annealing calculations were employed to generate structures for leucocin A, in both lipophilic media. While some differences were noted between the, structures calculated for the two different solvent systems, in both, the, region encompassing residues 17-31 assumes an essentially identical, amphiphilic alpha-helix conformation. A three-strand antiparallel, beta-sheet domain (residues 2-16), anchored by the disulfide bridge, is, also observed in both media. In TFE, these two regions have a more defined, relationship relative to each other, while, in DPC micelles, the, C-terminus is folded back onto the alpha-helix. The implications of these, structural features with regard to the antimicrobial mechanism of action, and target recognition are discussed.
+The first three-dimensional structure of a type IIa bacteriocin from lactic acid bacteria is reported. Complete 1H resonance assignments of leucocin A, a 37 amino acid antimicrobial peptide isolated from the lactic acid bacterium Leuconostoc gelidum UAL187, were determined in 90% trifluoroethanol (TFE)-water and in aqueous dodecylphosphocholine (DPC) micelles (1:40 ratio of leucocin A:DPC) using two-dimensional NMR techniques (e.g., DQF-COSY, TOCSY, NOESY). Circular dichroism spectra, NMR chemical shift indices, amide hydrogen exchange rates, and long-range nuclear Overhauser effects indicate that leucocin A adopts a reasonably well defined structure in both TFE and DPC micelle environments but exists as a random coil in water or aqueous DMSO. Distance geometry and simulated annealing calculations were employed to generate structures for leucocin A in both lipophilic media. While some differences were noted between the structures calculated for the two different solvent systems, in both, the region encompassing residues 17-31 assumes an essentially identical amphiphilic alpha-helix conformation. A three-strand antiparallel beta-sheet domain (residues 2-16), anchored by the disulfide bridge, is also observed in both media. In TFE, these two regions have a more defined relationship relative to each other, while, in DPC micelles, the C-terminus is folded back onto the alpha-helix. The implications of these structural features with regard to the antimicrobial mechanism of action and target recognition are discussed.
 ==About this Structure==
-LEU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leuconostoc_gelidum Leuconostoc gelidum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2LEU OCA].
+LEU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Leuconostoc_gelidum Leuconostoc gelidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEU OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Leuconostoc gelidum]]
 [[Category: Single protein]]
-[[Category: Gallagher, N.L.F.]]
+[[Category: Gallagher, N L.F.]]
-[[Category: Nakashima, T.T.]]
+[[Category: Nakashima, T T.]]
-[[Category: Niemczura, W.P.]]
+[[Category: Niemczura, W P.]]
 [[Category: Sailer, M.]]
-[[Category: Stiles, M.E.]]
+[[Category: Stiles, M E.]]
-[[Category: Vederas, J.C.]]
+[[Category: Vederas, J C.]]
 [[Category: antibacterial peptide]]
 [[Category: bacteriocin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:41:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:05 2008''