2c7e: Difference between revisions
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New page: left|200px<br /><applet load="2c7e" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c7e" /> '''REVISED ATOMIC STRUCTURE FITTING INTO A GROE... |
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[[Image:2c7e.gif|left|200px]]<br /><applet load="2c7e" size=" | [[Image:2c7e.gif|left|200px]]<br /><applet load="2c7e" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2c7e" /> | caption="2c7e" /> | ||
'''REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)'''<br /> | '''REVISED ATOMIC STRUCTURE FITTING INTO A GROEL(D398A)-ATP7 CRYO-EM MAP (EMD 1047)'''<br /> | ||
==Overview== | ==Overview== | ||
The chaperonin GroEL drives its protein-folding cycle by cooperatively | The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously discharging the previous folding chamber from the opposite ring. The GroEL-ATP structure, determined by cryo-EM and atomic structure fitting, shows that the intermediate domains rotate downward, switching their intersubunit salt bridge contacts from substrate binding to ATP binding domains. These observations, together with the effects of ATP binding to a GroEL-GroES-ADP complex, suggest structural models for the ATP-induced reduction in affinity for polypeptide and for cooperativity. The model for cooperativity, based on switching of intersubunit salt bridge interactions around the GroEL ring, may provide general insight into cooperativity in other ring complexes and molecular machines. | ||
==About this Structure== | ==About this Structure== | ||
2C7E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with K, MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | 2C7E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1GR6. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7E OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Farr, G | [[Category: Farr, G W.]] | ||
[[Category: Fenton, W | [[Category: Fenton, W A.]] | ||
[[Category: Gowen, B.]] | [[Category: Gowen, B.]] | ||
[[Category: Horwich, A | [[Category: Horwich, A L.]] | ||
[[Category: Ranson, N | [[Category: Ranson, N A.]] | ||
[[Category: Roseman, A | [[Category: Roseman, A M.]] | ||
[[Category: Saibil, H | [[Category: Saibil, H R.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: K]] | [[Category: K]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:48 2008'' | ||
