2nwc: Difference between revisions
New page: left|200px<br /><applet load="2nwc" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nwc, resolution 3.02Å" /> '''A 3.02 angstrom crys... |
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==Overview== | ==Overview== | ||
GroEL is a member of the ATP-dependent chaperonin family that promotes the | 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 Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions., Kiser PD, Lodowski DT, Palczewski K, Acta | Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions., Kiser PD, Lodowski DT, Palczewski K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):457-61. Epub 2007 May 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17554162 17554162] | ||
[[Category: Chaperonin ATPase]] | [[Category: Chaperonin ATPase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kiser, P | [[Category: Kiser, P D.]] | ||
[[Category: Lodowski, D | [[Category: Lodowski, D T.]] | ||
[[Category: Palczewski, K.]] | [[Category: Palczewski, K.]] | ||
[[Category: chaperonin]] | [[Category: chaperonin]] | ||
[[Category: hsp60]] | [[Category: hsp60]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:44 2008'' | ||
Revision as of 19:11, 21 February 2008
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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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):457-61. Epub 2007 May 5. PMID:17554162
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