2nwc
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A 3.02 angstrom crystal structure of wild-type apo GroEL in a monoclinic space group
OverviewOverview
GroEL is a member of the ATP-dependent chaperonin family that promotes the, proper folding of many cytosolic bacterial proteins. The structures of, GroEL in a variety of different states have been determined using X-ray, crystallography and cryo-electron microscopy. In this study, a 3.02 A, crystal structure of the native GroEL complex from Escherichia coli is, presented. The complex was purified and crystallized in the absence of, potassium ions, which allowed evaluation of the structural changes that, may occur in response to cognate potassium-ion binding by comparison to, the previously determined wild-type GroEL structure (PDB code 1xck), in, which potassium ions were observed in all 14 subunits. In general, the, structure is similar to the previously determined wild-type GroEL crystal, structure with some differences in regard to temperature-factor, distribution.
About this StructureAbout this Structure
2NWC is a Single protein structure of sequence from Escherichia coli. Active as Chaperonin ATPase, with EC number 3.6.4.9 Full crystallographic information is available from OCA.
ReferenceReference
Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions., Kiser PD, Lodowski DT, Palczewski K, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):457-61. Epub 2007 May 5. PMID:17554162
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