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| | <StructureSection load='1sg2' size='340' side='right'caption='[[1sg2]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='1sg2' size='340' side='right'caption='[[1sg2]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sg2]] is a 3 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=1SG2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SG2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sg2]] is a 3 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=1SG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SG2 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLPA, SKP, OMPH, B0178, C0215, Z0190, ECS0180, SF0168, S0171 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 2.35Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sg2 OCA], [http://pdbe.org/1sg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sg2 RCSB], [http://www.ebi.ac.uk/pdbsum/1sg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sg2 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=1sg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sg2 OCA], [https://pdbe.org/1sg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sg2 RCSB], [https://www.ebi.ac.uk/pdbsum/1sg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sg2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dommel, M K]] | + | [[Category: Dommel MK]] |
| - | [[Category: Korndorfer, I P]] | + | [[Category: Korndorfer IP]] |
| - | [[Category: Skerra, A]] | + | [[Category: Skerra A]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Hydrophobic surface]]
| + | |
| - | [[Category: Molecular dipole]]
| + | |
| - | [[Category: Outer membrane protein]]
| + | |
| - | [[Category: Protein folding]]
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| Structural highlights
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 17-kDa protein (Skp) of Escherichia coli is a homotrimeric periplasmic chaperone for newly synthesized outer-membrane proteins. Here we present its X-ray structure at a resolution of 2.35 A. Three hairpin-shaped alpha-helical extensions reach out by approximately 60 A from a trimerization domain, which is composed of three intersubunit beta-sheets that wind around a central axis. The alpha-helical extensions approach each other at their distal turns, resulting in a fold that resembles a 'three-pronged grasping forceps'. The overall shape of Skp is reminiscent of the cytosolic chaperone prefoldin, although it is based on a radically different topology. The peculiar architecture, with apparent plasticity of the prongs and distinct electrostatic and hydrophobic surface properties, supports the recently proposed biochemical mechanism of this chaperone: formation of a Skp(3)-Omp complex protects the outer membrane protein from aggregation during passage through the bacterial periplasm.
Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture.,Korndorfer IP, Dommel MK, Skerra A Nat Struct Mol Biol. 2004 Oct;11(10):1015-20. Epub 2004 Sep 12. PMID:15361861[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
- ↑ Korndorfer IP, Dommel MK, Skerra A. Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. Nat Struct Mol Biol. 2004 Oct;11(10):1015-20. Epub 2004 Sep 12. PMID:15361861 doi:10.1038/nsmb828
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