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Chaperonin, Sandbox transition test

From Proteopedia

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[[Image:1pcq.png|left|200px|thumb|Crystal Structure of Chaperonin, [[1pcq]]]]
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==Your Heading Here (maybe something like 'Structure')==
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{{STRUCTURE_1pcq| PDB=1pcq | SIZE=400| SCENE=Chaperonin/Groel_groes_comnplex/1 |right|CAPTION=GroEL/GroES complex, [[1pcq]] }}
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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This is a default text for your page '''Sandbox transition test'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Function ==
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== Disease ==
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<br>
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Load 1eve and save with standard defaults - no reload standard display YES YES transition <scene name='10/1050327/Sb_transition_default/1'>Default</scene>
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<br>
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blow up
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always reload YES YES <scene name='10/1050327/Sb_transition_default/2'>default blow up</scene>
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<br>
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no reload YES YES <scene name='10/1050327/Sb_transition_default/3'>NO Reload Blow up</scene>
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== Relevance ==
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== Structural highlights ==
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The X-ray structure of the E2020-''Tc''AChE complex shows that E2020 has a <scene name='1eve/E2020_close_up_with_84_279/13'>unique orientation</scene> along the active-site gorge, extending from the anionic subsite (<scene name='1eve/E2020_close_up_with_84lbld/7'>W84</scene>) of the active site, at the bottom, to the peripheral anionic site (<scene name='1eve/E2020_close_up_with_84_279lbld/5'>near W279</scene>), at the top, via aromatic stacking interactions with conserved aromatic acid residues. E2020 does not, however, interact directly with either the catalytic triad or the 'oxyanion hole' but only <scene name='1eve/E20_interactionshown/8'>indirectly via solvent molecules</scene>.
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</StructureSection>
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== References ==
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<references/>
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'''Chaperonins''' (CPN) are oligomeric proteins that mediate the folding of polypeptide chains. Group I CPN are found in bacteria, chloroplasts and mitochondria. For an introductory overview, see [http://en.wikipedia.org/wiki/Chaperonins Chaperonins in Wikipedia].
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The most characterized CPN are in the GroEL/GroES complex from ''Escherichia coli'' and CPN60/CPN10 from ''Thermus thermophilus''. The larger subunit (GroEL, CPN60) contains 3 domains. The apical domain is the one which binds the substrate. Group II CPNs are found in eukaryotic cytosol and archaea. Thermosome is a CPN complex found in archaea. CCT is a CPN complex found in eukarya.
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{{TOC limit|limit=2}}
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== 3D Structures of Chaperonin ==
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''Updated January 2013''
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===Group I===
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''Large subunit''
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[[3m6c]] – MtGroEL1 apical domain – ''Mycobacterium tuberculosis''<BR />
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[[1sjp]], [[3rtk]] – MtGroEL2 residues 42-539<BR />
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[[3fbh]], [[2eu1]], [[1j4z]], [[1kpo]], [[1oel]], [[1grl]], [[2yey]] – EcGroEL (mutant) - ''Escherichia coli''<BR />
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[[3e76]], [[2nwc]], [[1xck]], [[1ss8]] – EcGroEL<BR />
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[[3c9v]], [[3cau]], [[2ynj]] – EcGroEL – Cryo EM<BR />
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[[2c7e]], [[1gr5]], [[4aaq]] - EcGroEL (mutant) – Cryo EM<BR />
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[[1dk7]] - EcGroEL apical domain<br />
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[[1fy9]], [[1fya]], [[1kid]], [[1jon]] – EcGroEL apical domain (mutant) <BR />
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[[1srv]] – TtCPN60 apical domain - ''Thermus thermophilus''<BR />
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[[3osx]] - CPN60 apical domain – ''Xenorhabdus nematophila''<br />
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[[1iok]] – CPN60 – ''Paracoccus denitrificans''
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''Large subunit binary complex''
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[[1kp8]] - EcGroEL (mutant) + ATP<BR />
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[[4aar]], [[4aas]], [[4aau]], [[4ab2]], [[4ab3]] - EcGroEL (mutant) + ATP – Cryo EM<br />
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[[1sx3]] - EcGroEL + ATP<BR />
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[[1sx4]] - EcGroEL + ADP<BR />
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[[1mnf]] – EcGroEL + polypeptide<BR />
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[[2cgt]] – EcGroEL + capsid assbly protein GP31 – EM<BR />
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[[1dkd]] - EcGroEL apical domain + polypeptide
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''Small subunit''
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[[3nx6]] – GroES residues 40-134 (mutant) – ''Xanthomonas oryzae''<BR />
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[[1wnr]] – TtCPN10 residues 1-94<BR />
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[[1p3h]], [[1hx5]] – MtCPN10<BR />
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[[1p82]], [[1p83]] - MtCPN10 residues 1-25 - NMR<BR />
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[[1egs]] - GroES residues 19-27 - NMR
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''Large + small subunit''
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[[1svt]], [[1pcq]] - EcGroEL + GroES<BR />
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[[1pf9]], [[1aon]] - EcGroEL + GroES + ADP<BR />
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[[2c7c]], [[2c7d]] - EcGroEL + GroES – Cryo EM<BR />
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[[1gru]] - EcGroEL + GroES + ATP + ADP – Cryo EM<BR />
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[[1we3]] – TtCPN60 + CPN10<BR />
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[[1wf4]] - TtCPN60 + CPN10 + ADP
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===Group II===
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[[3izh]], [[3izi]], [[3izj]], [[3izk]], [[3izl]], [[3izm]], [[3izn]], [[3los]], [[3iyf]] – MmCPN – ''Methanococcus maripaludis'' – EM<BR />
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[[3kfb]], [[3kfe]], [[3kfk]] – MmCPN<BR />
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[[3j02]], [[3j03]] – MmCPN (mutant) – Cryo EM<br />
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[[3ruq]] - MmCPN + ADP<br />
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[[3rus]] - MmCPN (mutant) + ADP<br />
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[[3ruw]] - MmCPN (mutant) + ADP-AlF3<br />
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[[3ruv]] - MmCPN (mutant) + ATP analog<br />
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[[1q2v]], [[1q3r]] – TkCPN α subunit (mutant) – ''Thermococcus'' KS-1<BR />
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[[1q3q]] - TkCPN α subunit (mutant) + AMP-PNP<BR />
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[[1q3s]] - TkCPN α subunit (mutant) + ADP
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''CCT''
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[[2xsm]] – bCPN CCT – bovine<BR />
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[[3p9d]], [[3p9e]], [[4d8q]], [[4d8r]] – CPN CCT - yeast<br />
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[[3iyg]] - bCPN CCT – Cryo EM<BR />
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[[3ktt]] - bCPN CCT β subunit – Cryo EM<BR />
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[[1gml]], [[1gn1]] - CPN CCT γ subunit apical domain – mouse
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''Hsp33''
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[[3m7m]], [[1hw7]] – EcCPN Hsp33 N-terminal<BR />
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[[1xjh]] - EcCPN Hsp33 C terminal - NMR<BR />
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[[1vq0]] - CPN Hsp33 – ''Thermotoga maritima''<BR />
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[[1vzy]] - CPN Hsp33 (mutant) – ''Bacillus subtilis''
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''Thermosome''
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[[1a6d]] - TaTherm α+β subunits – ''Thermoplasma acidophilum''<BR />
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[[1a6e]] - TaTherm α+β subunits + ADP<BR />
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[[1ass]], [[1asx]] - TaTherm α apical domain<BR />
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[[1e0r]] – TaTherm β apical domain<br />
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[[3ko1]] – Therm – ''Acidianus tengchongensis''<br />
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[[3aq1]] – Therm – ''Methanococcoides burtonii''<br />
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[[1lep]] – CPN-10 – ''Mycobacterium leprae''
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[[Category:Topic Page]]
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Revision as of 10:35, 8 March 2026

Your Heading Here (maybe something like 'Structure')

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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