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1a6d

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Revision as of 09:42, 26 May 2021

THERMOSOME FROM T. ACIDOPHILUM

Structural highlights

1a6d is a 2 chain structure with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[THSA_THEAC] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. [THSB_THEAC] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We have determined to 2.6 A resolution the crystal structure of the thermosome, the archaeal group II chaperonin from T. acidophilum. The hexadecameric homolog of the eukaryotic chaperonin CCT/TRiC shows an (alphabeta)4(alphabeta)4 subunit assembly. Domain folds are homologous to GroEL but form a novel type of inter-ring contact. The domain arrangement resembles the GroEL-GroES cis-ring. Parts of the apical domains form a lid creating a closed conformation. The lid substitutes for a GroES-like cochaperonin that is absent in the CCT/TRiC system. The central cavity has a polar surface implicated in protein folding. Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the ATP form.

Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT.,Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S Cell. 1998 Apr 3;93(1):125-38. PMID:9546398^[1]

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

References

↑ Ditzel L, Lowe J, Stock D, Stetter KO, Huber H, Huber R, Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell. 1998 Apr 3;93(1):125-38. PMID:9546398

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a6d"

@@ Line 3: / Line 3: @@
 <StructureSection load='1a6d' size='340' side='right'caption='[[1a6d]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1a6d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A6D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1a6d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A6D FirstGlance]. <br>
-</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=1a6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6d OCA], [http://pdbe.org/1a6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a6d RCSB], [http://www.ebi.ac.uk/pdbsum/1a6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6d ProSAT]</span></td></tr>
+</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=1a6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6d OCA], [https://pdbe.org/1a6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a6d RCSB], [https://www.ebi.ac.uk/pdbsum/1a6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/THSA_THEAC THSA_THEAC]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. [[http://www.uniprot.org/uniprot/THSB_THEAC THSB_THEAC]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
+[[https://www.uniprot.org/uniprot/THSA_THEAC THSA_THEAC]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity. [[https://www.uniprot.org/uniprot/THSB_THEAC THSB_THEAC]] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1a6d

From Proteopedia

Revision as of 09:42, 26 May 2021

THERMOSOME FROM T. ACIDOPHILUM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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