1a6d: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /><applet load="1a6d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a6d, resolution 2.6Å" /> '''THERMOSOME FROM T. AC...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1a6d.gif|left|200px]]<br /><applet load="1a6d" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1a6d, resolution 2.6&Aring;" />
'''THERMOSOME FROM T. ACIDOPHILUM'''<br />


==Overview==
==THERMOSOME FROM T. ACIDOPHILUM==
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.
<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 [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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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 ==
[https://www.uniprot.org/uniprot/THSA_THEAC THSA_THEAC] Molecular chaperone; binds unfolded polypeptides in vitro, and has a weak ATPase activity.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a6/1a6d_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a6d ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1A6D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6D OCA].
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9546398 9546398]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
[[Category: Ditzel, L.]]
[[Category: Ditzel L]]
[[Category: Huber, H.]]
[[Category: Huber H]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Loewe, J.]]
[[Category: Loewe J]]
[[Category: Steinbacher, S.]]
[[Category: Steinbacher S]]
[[Category: Stetter, K.O.]]
[[Category: Stetter K-O]]
[[Category: Stock, D.]]
[[Category: Stock D]]
[[Category: atpase]]
[[Category: cct]]
[[Category: group ii chaperonin]]
[[Category: protein folding]]
[[Category: thermoplasma acidophilum]]
[[Category: tric]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:38:19 2007''

Latest revision as of 06:28, 7 February 2024

THERMOSOME FROM T. ACIDOPHILUM

1a6d, resolution 2.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1a6d&oldid=4039919"