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1u2m

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Revision as of 18:29, 25 December 2014

Crystal Structure of Skp

Structural highlights

1u2m is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	HLPA (Escherichia coli)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[SKP_ECOLI] Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane.^[1] ^[2] ^[3] ^[4] ^[5]

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

The Seventeen Kilodalton Protein (Skp) is a trimeric periplasmic chaperone that assists outer membrane proteins in their folding and insertion into membranes. Here we report the crystal structure of Skp from E. coli. The structure of the Skp trimer resembles a jellyfish with alpha-helical tentacles protruding from a beta barrel body defining a central cavity. The architecture of Skp is unexpectedly similar to that of Prefoldin/GimC, a cytosolic chaperone present in eukaria and archea, that binds unfolded substrates in its central cavity. The ability of Skp to prevent the aggregation of model substrates in vitro is independent of ATP. Skp can interact directly with membrane lipids and lipopolysaccharide (LPS). These interactions are needed for efficient Skp-assisted folding of membrane proteins. We have identified a putative LPS binding site on the outer surface of Skp and propose a model for unfolded substrate binding.

Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation.,Walton TA, Sousa MC Mol Cell. 2004 Aug 13;15(3):367-74. PMID:15304217^[6]

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

References

↑ Chen R, Henning U. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol. 1996 Mar;19(6):1287-94. PMID:8730870
↑ De Cock H, Schafer U, Potgeter M, Demel R, Muller M, Tommassen J. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur J Biochem. 1999 Jan;259(1-2):96-103. PMID:9914480
↑ Schafer U, Beck K, Muller M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J Biol Chem. 1999 Aug 27;274(35):24567-74. PMID:10455120
↑ Harms N, Koningstein G, Dontje W, Muller M, Oudega B, Luirink J, de Cock H. The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J Biol Chem. 2001 Jun 1;276(22):18804-11. Epub 2001 Mar 5. PMID:11278858 doi:http://dx.doi.org/10.1074/jbc.M011194200
↑ Bulieris PV, Behrens S, Holst O, Kleinschmidt JH. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J Biol Chem. 2003 Mar 14;278(11):9092-9. Epub 2002 Dec 30. PMID:12509434 doi:http://dx.doi.org/10.1074/jbc.M211177200
↑ Walton TA, Sousa MC. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol Cell. 2004 Aug 13;15(3):367-74. PMID:15304217 doi:10.1016/j.molcel.2004.07.023

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/1u2m"

Categories: Escherichia coli | Sousa, M C | Walton, T A | Chaperone

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1u2m]] is a 3 chain structure with 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=1U2M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U2M FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u2m RCSB], [http://www.ebi.ac.uk/pdbsum/1u2m PDBsum]</span></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=1u2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u2m RCSB], [http://www.ebi.ac.uk/pdbsum/1u2m PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SKP_ECOLI SKP_ECOLI]] Molecular chaperone that interacts specifically with outer membrane proteins, thus maintaining the solubility of early folding intermediates during passage through the periplasm. Required for the efficient release of OmpA from the inner membrane, the maintenance of its solubility in the periplasm, and, in association with lipopolysaccharide (LPS), for the efficient folding and insertion of OmpA into the outer membrane.<ref>PMID:8730870</ref> <ref>PMID:9914480</ref> <ref>PMID:10455120</ref> <ref>PMID:11278858</ref> <ref>PMID:12509434</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 </StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Sousa, M C.]]
+[[Category: Sousa, M C]]
-[[Category: Walton, T A.]]
+[[Category: Walton, T A]]
 [[Category: Chaperone]]

1u2m

From Proteopedia

Revision as of 18:29, 25 December 2014

Crystal Structure of Skp

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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