1eq7: Difference between revisions

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<StructureSection load='1eq7' size='340' side='right'caption='[[1eq7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1eq7' size='340' side='right'caption='[[1eq7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1eq7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQ7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1eq7]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EQ7 FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq7 OCA], [https://pdbe.org/1eq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eq7 RCSB], [https://www.ebi.ac.uk/pdbsum/1eq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eq7 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eq7 OCA], [https://pdbe.org/1eq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eq7 RCSB], [https://www.ebi.ac.uk/pdbsum/1eq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eq7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/LPP_ECOLI LPP_ECOLI]] Interacts with the peptidoglycan both covalently and noncovalently. This interaction contributes to the maintenance of the structural and functional integrity of the cell envelope.  
[https://www.uniprot.org/uniprot/LPP_ECOLI LPP_ECOLI] Interacts with the peptidoglycan both covalently and noncovalently. This interaction contributes to the maintenance of the structural and functional integrity of the cell envelope.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eq7 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eq7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:10843861</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1eq7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ji, H]]
[[Category: Ji H]]
[[Category: Liu, J]]
[[Category: Liu J]]
[[Category: Lu, M]]
[[Category: Lu M]]
[[Category: Shu, W]]
[[Category: Shu W]]
[[Category: Helix capping]]
[[Category: Lipoprotein]]
[[Category: Membrane protein]]
[[Category: Outer membrane]]
[[Category: Protein folding]]
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