1eq7: Difference between revisions

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[[Image:1eq7.gif|left|200px]]<br /><applet load="1eq7" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1eq7.gif|left|200px]]<br /><applet load="1eq7" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1eq7, resolution 1.90Å" />

'''CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION'''<br />

==Overview==

The outer membrane lipoprotein of the Escherichia coli cell envelope has, characteristic lipid modifications at an amino-terminal cysteine and can, exist in a form bound covalently to the peptidoglycan through a, carboxyl-terminal lysine. The 56-residue polypeptide moiety of the, lipoprotein, designated Lpp-56, folds into a stable, trimeric helical, structure in aqueous solution. The 1.9 A resolution crystal structure of, Lpp-56 comprises a parallel three-stranded coiled coil including a novel, alanine-zipper unit and two helix-capping motifs. The amino-terminal motif, forms a hydrogen-bonding network anchoring an umbrella-shaped fold. The, carboxyl-terminal motif uses puckering of the tyrosine side-chains as a, unique docking arrangement in helix termination. The structure provides an, explanation for assembly and insertion of the lipoprotein molecules into, the outer membrane of gram-negative bacteria and suggests a molecular, target for antibacterial drug discovery.

The outer membrane lipoprotein of the Escherichia coli cell envelope has characteristic lipid modifications at an amino-terminal cysteine and can exist in a form bound covalently to the peptidoglycan through a carboxyl-terminal lysine. The 56-residue polypeptide moiety of the lipoprotein, designated Lpp-56, folds into a stable, trimeric helical structure in aqueous solution. The 1.9 A resolution crystal structure of Lpp-56 comprises a parallel three-stranded coiled coil including a novel alanine-zipper unit and two helix-capping motifs. The amino-terminal motif forms a hydrogen-bonding network anchoring an umbrella-shaped fold. The carboxyl-terminal motif uses puckering of the tyrosine side-chains as a unique docking arrangement in helix termination. The structure provides an explanation for assembly and insertion of the lipoprotein molecules into the outer membrane of gram-negative bacteria and suggests a molecular target for antibacterial drug discovery.

==About this Structure==

1EQ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1EQ7 OCA].

1EQ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ7 OCA].

==Reference==

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[[Category: protein folding]]

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@@ Line 1: / Line 1: @@
-[[Image:1eq7.gif|left|200px]]<br /><applet load="1eq7" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1eq7.gif|left|200px]]<br /><applet load="1eq7" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1eq7, resolution 1.90&Aring;" />
 '''CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION'''<br />
 ==Overview==
-The outer membrane lipoprotein of the Escherichia coli cell envelope has, characteristic lipid modifications at an amino-terminal cysteine and can, exist in a form bound covalently to the peptidoglycan through a, carboxyl-terminal lysine. The 56-residue polypeptide moiety of the, lipoprotein, designated Lpp-56, folds into a stable, trimeric helical, structure in aqueous solution. The 1.9 A resolution crystal structure of, Lpp-56 comprises a parallel three-stranded coiled coil including a novel, alanine-zipper unit and two helix-capping motifs. The amino-terminal motif, forms a hydrogen-bonding network anchoring an umbrella-shaped fold. The, carboxyl-terminal motif uses puckering of the tyrosine side-chains as a, unique docking arrangement in helix termination. The structure provides an, explanation for assembly and insertion of the lipoprotein molecules into, the outer membrane of gram-negative bacteria and suggests a molecular, target for antibacterial drug discovery.
+The outer membrane lipoprotein of the Escherichia coli cell envelope has characteristic lipid modifications at an amino-terminal cysteine and can exist in a form bound covalently to the peptidoglycan through a carboxyl-terminal lysine. The 56-residue polypeptide moiety of the lipoprotein, designated Lpp-56, folds into a stable, trimeric helical structure in aqueous solution. The 1.9 A resolution crystal structure of Lpp-56 comprises a parallel three-stranded coiled coil including a novel alanine-zipper unit and two helix-capping motifs. The amino-terminal motif forms a hydrogen-bonding network anchoring an umbrella-shaped fold. The carboxyl-terminal motif uses puckering of the tyrosine side-chains as a unique docking arrangement in helix termination. The structure provides an explanation for assembly and insertion of the lipoprotein molecules into the outer membrane of gram-negative bacteria and suggests a molecular target for antibacterial drug discovery.
 ==About this Structure==
-EQ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EQ7 OCA].
+EQ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ7 OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: protein folding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:13:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:24 2008''