1asx

From Proteopedia

(Difference between revisions)

Revision as of 10:35, 15 November 2017

APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM

Structural highlights

1asx is a 1 chain structure with sequence from "thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1ass
Gene:	THSA ("Thermoplasma acidophila" (sic) Darland et al. 1970)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[THSA_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

The crystal structure of the substrate binding domain of the thermosome, the archaeal group II chaperonin, has been determined at 2.3 A resolution. The core resembles the apical domain of GroEL but lacks the hydrophobic residues implied in binding of substrates to group I chaperonins. Rather, a large hydrophobic surface patch is found in a novel helix-turn-helix motif, which is characteristic of all group II chaperonins including the eukaryotic TRiC/CCT complex. Models of the holochaperonin, which are consistent with cryo electron microscopy data, suggest a dual role of this helical protrusion in substrate binding and controlling access to the central cavity independent of a GroES-like cochaperonin.

Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin.,Klumpp M, Baumeister W, Essen LO Cell. 1997 Oct 17;91(2):263-70. PMID:9346243^[1]

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

References

↑ Klumpp M, Baumeister W, Essen LO. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell. 1997 Oct 17;91(2):263-70. PMID:9346243

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM==
 <StructureSection load='1asx' size='340' side='right' caption='[[1asx]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ass|1ass]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">THSA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</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=1asx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1asx OCA], [http://pdbe.org/1asx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1asx RCSB], [http://www.ebi.ac.uk/pdbsum/1asx PDBsum]</span></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=1asx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1asx OCA], [http://pdbe.org/1asx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1asx RCSB], [http://www.ebi.ac.uk/pdbsum/1asx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1asx ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1asx" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Chaperonin|Chaperonin]]
-*[[Heat Shock Proteins|Heat Shock Proteins]]
 == References ==
 <references/>

1asx

From Proteopedia

Revision as of 10:35, 15 November 2017

APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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