1sg2

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[[Image:1sg2.gif|left|200px]]
[[Image:1sg2.gif|left|200px]]
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{{Structure
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|PDB= 1sg2 |SIZE=350|CAPTION= <scene name='initialview01'>1sg2</scene>, resolution 2.35&Aring;
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|GENE= 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 Escherichia coli])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sg2 OCA], [http://www.ebi.ac.uk/pdbsum/1sg2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sg2 RCSB]</span>
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'''Crystal structure of the periplasmic chaperone Skp'''
'''Crystal structure of the periplasmic chaperone Skp'''
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[[Category: Korndorfer, I P.]]
[[Category: Korndorfer, I P.]]
[[Category: Skerra, A.]]
[[Category: Skerra, A.]]
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[[Category: hydrophobic surface]]
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[[Category: Hydrophobic surface]]
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[[Category: molecular dipole]]
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[[Category: Molecular dipole]]
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[[Category: outer membrane protein]]
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[[Category: Outer membrane protein]]
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[[Category: protein folding]]
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[[Category: Protein folding]]
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Revision as of 05:39, 3 May 2008

Template:STRUCTURE 1sg2

Crystal structure of the periplasmic chaperone Skp


Overview

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.

About this Structure

1SG2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 08:39:34 2008

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