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1kfm

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Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants

Structural highlights

1kfm is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Native proteins exhibit precise geometric packing of atoms in their hydrophobic interiors. Nonetheless, controversy remains about the role of core side-chain packing in specifying and stabilizing the folded structures of proteins. Here we investigate the role of core packing in determining the conformation and stability of the Lpp-56 trimerization domain. The X-ray crystal structures of Lpp-56 mutants with alanine substitutions at two and four interior core positions reveal trimeric coiled coils in which the twist of individual helices and the helix-helix spacing vary significantly to achieve the most favored superhelical packing arrangement. Introduction of each alanine "layer" into the hydrophobic core destabilizes the superhelix by 1.4 kcal mol(-1). Although the methyl groups of the alanine residues pack at their optimum van der Waals contacts in the coiled-coil trimer, they provide a smaller component of hydrophobic interactions than bulky hydrophobic side-chains to the thermodynamic stability. Thus, specific side-chain packing in the hydrophobic core of coiled coils are important determinants of protein main-chain conformation and stability.

Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants.,Liu J, Cao W, Lu M J Mol Biol. 2002 May 3;318(3):877-88. PMID:12054830^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liu J, Cao W, Lu M. Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants. J Mol Biol. 2002 May 3;318(3):877-88. PMID:12054830 doi:10.1016/S0022-2836(02)00138-9

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kfm"

Categories: Escherichia coli | Large Structures | Cao W | Liu J | Lu M

@@ Line 3: / Line 3: @@
 <StructureSection load='1kfm' size='340' side='right'caption='[[1kfm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kfm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kfm]] 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=1KFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFM FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eq7|1eq7]], [[1jcb|1jcb]], [[1kfn|1kfn]]</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]] 2&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfm OCA], [http://pdbe.org/1kfm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kfm RCSB], [http://www.ebi.ac.uk/pdbsum/1kfm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfm ProSAT]</span></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=1kfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfm OCA], [https://pdbe.org/1kfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfm RCSB], [https://www.ebi.ac.uk/pdbsum/1kfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Cao, W]]
+[[Category: Cao W]]
-[[Category: Liu, J]]
+[[Category: Liu J]]
-[[Category: Lu, M]]
+[[Category: Lu M]]
-[[Category: Alanine-zipper]]
-[[Category: Helix capping]]
-[[Category: Lipoprotein]]
-[[Category: Membrane protein]]
-[[Category: Protein folding]]

1kfm

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Current revision

Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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