5opx

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the GroEL mutant A109C in complex with GroES and ADP BeF2

Structural highlights

5opx is a 28 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.64Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate protein (SP) to fold in isolation. GroEL and GroES undergo an ATP-regulated interaction cycle to close and open the folding cage. GroEL consists of two heptameric rings stacked back to back. Here, we show that GroEL undergoes transient ring separation, resulting in ring exchange between complexes. Ring separation occurs upon ATP-binding to the trans ring of the asymmetric GroEL:7ADP:GroES complex in the presence or absence of SP and is a consequence of inter-ring negative allostery. We find that a GroEL mutant unable to perform ring separation is folding active but populates symmetric GroEL:GroES2 complexes, where both GroEL rings function simultaneously rather than sequentially. As a consequence, SP binding and release from the folding chamber is inefficient, and E. coli growth is impaired. We suggest that transient ring separation is an integral part of the chaperonin mechanism.

GroEL Ring Separation and Exchange in the Chaperonin Reaction.,Yan X, Shi Q, Bracher A, Milicic G, Singh AK, Hartl FU, Hayer-Hartl M Cell. 2017 Dec 26. pii: S0092-8674(17)31490-3. doi: 10.1016/j.cell.2017.12.010. PMID:29336887^[1]

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

References

↑ Yan X, Shi Q, Bracher A, Milicic G, Singh AK, Hartl FU, Hayer-Hartl M. GroEL Ring Separation and Exchange in the Chaperonin Reaction. Cell. 2017 Dec 26. pii: S0092-8674(17)31490-3. doi: 10.1016/j.cell.2017.12.010. PMID:29336887 doi:http://dx.doi.org/10.1016/j.cell.2017.12.010

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/5opx"

@@ Line 3: / Line 3: @@
 <StructureSection load='5opx' size='340' side='right'caption='[[5opx]], [[Resolution|resolution]] 3.64&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5opx]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OPX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OPX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5opx]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OPX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.64&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">groL, groEL, mopA, b4143, JW4103 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), groS, groES, mopB, b4142, JW4102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<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=5opx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5opx OCA], [http://pdbe.org/5opx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5opx RCSB], [http://www.ebi.ac.uk/pdbsum/5opx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5opx ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5opx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5opx OCA], [https://pdbe.org/5opx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5opx RCSB], [https://www.ebi.ac.uk/pdbsum/5opx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5opx ProSAT]</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]
+[https://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]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Bracher, A]]
+[[Category: Bracher A]]
-[[Category: Hartl, F U]]
+[[Category: Hartl FU]]
-[[Category: Hayer-Hartl, M]]
+[[Category: Hayer-Hartl M]]
-[[Category: Milicic, G]]
+[[Category: Milicic G]]
-[[Category: Shi, Q]]
+[[Category: Shi Q]]
-[[Category: Singh, A K]]
+[[Category: Singh AK]]
-[[Category: Yan, X]]
+[[Category: Yan X]]
-[[Category: Chaperone]]
-[[Category: Chaperonin]]

5opx

From Proteopedia

Current revision

Crystal structure of the GroEL mutant A109C in complex with GroES and ADP BeF2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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