We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1p3h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1p3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p3h, resolution 2.8&Aring;" /> '''Crystal Structure of ...)
Current revision (08:04, 14 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1p3h.gif|left|200px]]<br /><applet load="1p3h" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1p3h, resolution 2.8&Aring;" />
 
-
'''Crystal Structure of the Mycobacterium tuberculosis chaperonin 10 tetradecamer'''<br />
 
-
==Overview==
+
==Crystal Structure of the Mycobacterium tuberculosis chaperonin 10 tetradecamer==
-
The crystal structure of Mycobacterium tuberculosis chaperonin 10, (cpn10(Mt)) has been determined to a resolution of 2.8 A. Two dome-shaped, cpn10(Mt) heptamers complex through loops at their bases to form a, tetradecamer with 72 symmetry and a spherical cage-like structure. The, hollow interior enclosed by the tetradecamer is lined with hydrophilic, residues and has dimensions of 30 A perpendicular to and 60 A along the, sevenfold axis. Tetradecameric cpn10(Mt) has also been observed in, solution by dynamic light scattering. Through its base loop sequence, cpn10(Mt) is known to be the agent in the bacterium responsible for bone, resorption and for the contribution towards its strong T-cell, immunogenicity. Superimposition of the cpn10(Mt) sequences 26 to 32 and 66, to 72 and E. coli GroES 25 to 31 associated with bone resorption activity, shows them to have similar conformations and structural features, suggesting that there may be a common receptor for the bone resorption, sequences. The base loops of cpn10s in general also attach to the, corresponding chaperonin 60 (cpn60) to enclose unfolded protein and to, facilitate its correct folding in vivo. Electron density corresponding to, a partially disordered protein subunit appears encapsulated within the, interior dome cavity of each heptamer. This suggests that the binding of, substrates to cpn10 is possible in the absence of cpn60.
+
<StructureSection load='1p3h' size='340' side='right'caption='[[1p3h]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1p3h]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jh2 1jh2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P3H 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]] 2.8&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=1p3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p3h OCA], [https://pdbe.org/1p3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p3h RCSB], [https://www.ebi.ac.uk/pdbsum/1p3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p3h ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CH10_MYCTU CH10_MYCTU] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580]
 +
== 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/p3/1p3h_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=1p3h ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1P3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with CA and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1JH2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P3H OCA].
+
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops., Roberts MM, Coker AR, Fossati G, Mascagni P, Coates AR, Wood SP, J Bacteriol. 2003 Jul;185(14):4172-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12837792 12837792]
+
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
-
[[Category: Single protein]]
+
[[Category: Coates ARM]]
-
[[Category: Coates, A.R.M.]]
+
[[Category: Coker AR]]
-
[[Category: Coker, A.R.]]
+
[[Category: Fossati G]]
-
[[Category: Fossati, G.]]
+
[[Category: Mascagni P]]
-
[[Category: Mascagni, P.]]
+
[[Category: Roberts MM]]
-
[[Category: Roberts, M.M.]]
+
[[Category: Wood SP]]
-
[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
+
-
[[Category: Wood, S.P.]]
+
-
[[Category: CA]]
+
-
[[Category: MPD]]
+
-
[[Category: acidic cluster]]
+
-
[[Category: beta barrel]]
+
-
[[Category: flexible loop]]
+
-
[[Category: protein structure initiative]]
+
-
[[Category: psi]]
+
-
[[Category: structural genomics]]
+
-
[[Category: tb structural genomics consortium]]
+
-
[[Category: tbsgc]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:26:36 2007''
+

Current revision

Crystal Structure of the Mycobacterium tuberculosis chaperonin 10 tetradecamer

PDB ID 1p3h

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools