1mqy: Difference between revisions

Line 1:

[[Image:1mqy.jpg|left|200px]]<br /><applet load="1mqy" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1mqy.jpg|left|200px]]<br /><applet load="1mqy" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1mqy" />

'''NMR solution structure of type-B lantibiotics mersacidin in DPC micelles'''<br />

==Overview==

Mersacidin belongs to the type B lantibiotics (lanthionine-containing, antibiotics) that contain post-translationally modified amino acids and, cyclic ring structures. It targets the cell wall precursor lipid II and, thereby inhibits cell wall synthesis. In light of the emerging antibiotics, resistance problem, the understanding of the antibacterial activity on a, structural basis provides a key to circumvent this issue. Here we present, solution NMR studies of mersacidin-lipid II interaction in, dodecylphosphocholine (DPC) micelles. Distinct solution structures of, mersacidin were determined in three different states: in water/methanol, solution and in DPC micelles with and without lipid II. The structures in, various sample conditions reveal remarkable conformational changes in, which the junction between Ala-12 and Abu-13 (where Abu is aminobutyric, acid) effectively serves as the hinge for the opening and closure of the, ring structures. The DPC micelle-bound form resembles the previously, determined NMR and x-ray crystal structures of mersacidin in pure methanol, but substantially deviates from the other two states in our current, report. The structural changes delineate the large chemical shift, perturbations observed during the course of a two-step (15)N-(1)H, heteronuclear single quantum coherence titration. They also modulate the, surface charge distribution of mersacidin suggesting that electrostatics, play a central role in the mersacidin-lipid II interaction. The observed, conformational adaptability of mersacidin might be a general feature of, lipid II-interacting antibiotics/peptides.

Mersacidin belongs to the type B lantibiotics (lanthionine-containing antibiotics) that contain post-translationally modified amino acids and cyclic ring structures. It targets the cell wall precursor lipid II and thereby inhibits cell wall synthesis. In light of the emerging antibiotics resistance problem, the understanding of the antibacterial activity on a structural basis provides a key to circumvent this issue. Here we present solution NMR studies of mersacidin-lipid II interaction in dodecylphosphocholine (DPC) micelles. Distinct solution structures of mersacidin were determined in three different states: in water/methanol solution and in DPC micelles with and without lipid II. The structures in various sample conditions reveal remarkable conformational changes in which the junction between Ala-12 and Abu-13 (where Abu is aminobutyric acid) effectively serves as the hinge for the opening and closure of the ring structures. The DPC micelle-bound form resembles the previously determined NMR and x-ray crystal structures of mersacidin in pure methanol but substantially deviates from the other two states in our current report. The structural changes delineate the large chemical shift perturbations observed during the course of a two-step (15)N-(1)H heteronuclear single quantum coherence titration. They also modulate the surface charge distribution of mersacidin suggesting that electrostatics play a central role in the mersacidin-lipid II interaction. The observed conformational adaptability of mersacidin might be a general feature of lipid II-interacting antibiotics/peptides.

==About this Structure==

1MQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1MQY OCA].

1MQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQY OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Bierbaum, G.]]

[[Category: Bonvin, A.M.]]

[[Category: Bonvin, A M.]]

[[Category: Breukink, E.]]

[[Category: Hsu, S.T.]]

[[Category: Hsu, S T.]]

[[Category: Kaptein, R.]]

[[Category: Kruijff, B.de.]]

[[Category: Kruijff, B de.]]

[[Category: Nuland, N.A.van.]]

[[Category: Nuland, N A.van.]]

[[Category: Sahl, H.G.]]

[[Category: Sahl, H G.]]

[[Category: lantibiotics]]

[[Category: peptidoglycan]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sat Nov 24~~ 21:52:~~33 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:12 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1mqy.jpg|left|200px]]<br /><applet load="1mqy" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1mqy.jpg|left|200px]]<br /><applet load="1mqy" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1mqy" />
 '''NMR solution structure of type-B lantibiotics mersacidin in DPC micelles'''<br />
 ==Overview==
-Mersacidin belongs to the type B lantibiotics (lanthionine-containing, antibiotics) that contain post-translationally modified amino acids and, cyclic ring structures. It targets the cell wall precursor lipid II and, thereby inhibits cell wall synthesis. In light of the emerging antibiotics, resistance problem, the understanding of the antibacterial activity on a, structural basis provides a key to circumvent this issue. Here we present, solution NMR studies of mersacidin-lipid II interaction in, dodecylphosphocholine (DPC) micelles. Distinct solution structures of, mersacidin were determined in three different states: in water/methanol, solution and in DPC micelles with and without lipid II. The structures in, various sample conditions reveal remarkable conformational changes in, which the junction between Ala-12 and Abu-13 (where Abu is aminobutyric, acid) effectively serves as the hinge for the opening and closure of the, ring structures. The DPC micelle-bound form resembles the previously, determined NMR and x-ray crystal structures of mersacidin in pure methanol, but substantially deviates from the other two states in our current, report. The structural changes delineate the large chemical shift, perturbations observed during the course of a two-step (15)N-(1)H, heteronuclear single quantum coherence titration. They also modulate the, surface charge distribution of mersacidin suggesting that electrostatics, play a central role in the mersacidin-lipid II interaction. The observed, conformational adaptability of mersacidin might be a general feature of, lipid II-interacting antibiotics/peptides.
+Mersacidin belongs to the type B lantibiotics (lanthionine-containing antibiotics) that contain post-translationally modified amino acids and cyclic ring structures. It targets the cell wall precursor lipid II and thereby inhibits cell wall synthesis. In light of the emerging antibiotics resistance problem, the understanding of the antibacterial activity on a structural basis provides a key to circumvent this issue. Here we present solution NMR studies of mersacidin-lipid II interaction in dodecylphosphocholine (DPC) micelles. Distinct solution structures of mersacidin were determined in three different states: in water/methanol solution and in DPC micelles with and without lipid II. The structures in various sample conditions reveal remarkable conformational changes in which the junction between Ala-12 and Abu-13 (where Abu is aminobutyric acid) effectively serves as the hinge for the opening and closure of the ring structures. The DPC micelle-bound form resembles the previously determined NMR and x-ray crystal structures of mersacidin in pure methanol but substantially deviates from the other two states in our current report. The structural changes delineate the large chemical shift perturbations observed during the course of a two-step (15)N-(1)H heteronuclear single quantum coherence titration. They also modulate the surface charge distribution of mersacidin suggesting that electrostatics play a central role in the mersacidin-lipid II interaction. The observed conformational adaptability of mersacidin might be a general feature of lipid II-interacting antibiotics/peptides.
 ==About this Structure==
-MQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MQY OCA].
+MQY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQY OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Bierbaum, G.]]
-[[Category: Bonvin, A.M.]]
+[[Category: Bonvin, A M.]]
 [[Category: Breukink, E.]]
-[[Category: Hsu, S.T.]]
+[[Category: Hsu, S T.]]
 [[Category: Kaptein, R.]]
-[[Category: Kruijff, B.de.]]
+[[Category: Kruijff, B de.]]
-[[Category: Nuland, N.A.van.]]
+[[Category: Nuland, N A.van.]]
-[[Category: Sahl, H.G.]]
+[[Category: Sahl, H G.]]
 [[Category: lantibiotics]]
 [[Category: peptidoglycan]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:52:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:12 2008''