3zq0

From Proteopedia

(Difference between revisions)

Revision as of 17:43, 25 December 2014

Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein

Structural highlights

3zq0 is a 21 chain structure with sequence from Escherichia coli bl21 and Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	3zpz, 3zq1
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600] [CH10_ECOLI] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]

Publication Abstract from PubMed

The GroEL/ES chaperonin system is required for the assisted folding of many proteins. How these substrate proteins are encapsulated within the GroEL-GroES cavity is poorly understood. Using symmetry-free, single-particle cryo-electron microscopy, we have characterized a chemically modified mutant of GroEL (EL43Py) that is trapped at a normally transient stage of substrate protein encapsulation. We show that the symmetric pattern of the GroEL subunits is broken as the GroEL cis-ring apical domains reorient to accommodate the simultaneous binding of GroES and an incompletely folded substrate protein (RuBisCO). The collapsed RuBisCO folding intermediate binds to the lower segment of two apical domains, as well as to the normally unstructured GroEL C-terminal tails. A comparative structural analysis suggests that the allosteric transitions leading to substrate protein release and folding involve concerted shifts of GroES and the GroEL apical domains and C-terminal tails.

Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein.,Chen DH, Madan D, Weaver J, Lin Z, Schroder GF, Chiu W, Rye HS Cell. 2013 Jun 6;153(6):1354-65. doi: 10.1016/j.cell.2013.04.052. PMID:23746846^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chen DH, Madan D, Weaver J, Lin Z, Schroder GF, Chiu W, Rye HS. Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein. Cell. 2013 Jun 6;153(6):1354-65. doi: 10.1016/j.cell.2013.04.052. PMID:23746846 doi:10.1016/j.cell.2013.04.052

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zq0"

@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zq0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zq0 RCSB], [http://www.ebi.ac.uk/pdbsum/3zq0 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600]  Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600] [[http://www.uniprot.org/uniprot/CH10_ECOLI CH10_ECOLI]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3zq0

From Proteopedia

Revision as of 17:43, 25 December 2014

Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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