1sg2

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[[Image:1sg2.gif|left|200px]]
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{{STRUCTURE_1sg2| PDB=1sg2 | SCENE= }}
{{STRUCTURE_1sg2| PDB=1sg2 | SCENE= }}
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'''Crystal structure of the periplasmic chaperone Skp'''
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===Crystal structure of the periplasmic chaperone Skp===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15361861 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15361861}}
==About this Structure==
==About this Structure==
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[[Category: Outer membrane protein]]
[[Category: Outer membrane protein]]
[[Category: Protein folding]]
[[Category: Protein folding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:39:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:25:15 2008''

Revision as of 12:25, 28 July 2008

Image:1sg2.png

Template:STRUCTURE 1sg2

Crystal structure of the periplasmic chaperone Skp

Template:ABSTRACT PUBMED 15361861

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

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