1eq7
From Proteopedia
(New page: 200px<br /><applet load="1eq7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eq7, resolution 1.90Å" /> '''CORE STRUCTURE OF TH...) |
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| - | [[Image:1eq7.gif|left|200px]]<br /><applet load="1eq7" size=" | + | [[Image:1eq7.gif|left|200px]]<br /><applet load="1eq7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1eq7, resolution 1.90Å" /> | caption="1eq7, resolution 1.90Å" /> | ||
'''CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION'''<br /> | '''CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The outer membrane lipoprotein of the Escherichia coli cell envelope has | + | 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== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: protein folding]] | [[Category: protein folding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:24 2008'' |
Revision as of 10:30, 21 February 2008
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CORE STRUCTURE OF THE OUTER MEMBRANE LIPOPROTEIN FROM ESCHERICHIA COLI AT 1.9 ANGSTROM RESOLUTION
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.
About this Structure
1EQ7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution., Shu W, Liu J, Ji H, Lu M, J Mol Biol. 2000 Jun 16;299(4):1101-12. PMID:10843861
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