3kth: Difference between revisions

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-{{Seed}}
-[[Image:3kth.jpg|left|200px]]
-<!--
+==Structure of ClpP from Bacillus subtilis in orthorombic crystal form==
-The line below this paragraph, containing "STRUCTURE_3kth", creates the "Structure Box" on the page.
+<StructureSection load='3kth' size='340' side='right'caption='[[3kth]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3kth]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KTH FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#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=3kth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kth OCA], [https://pdbe.org/3kth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kth RCSB], [https://www.ebi.ac.uk/pdbsum/3kth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kth ProSAT]</span></td></tr>
-{{STRUCTURE_3kth|  PDB=3kth  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CLPP_BACSU CLPP_BACSU] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the Site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor.<ref>PMID:16899079</ref>
+== 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/kt/3kth_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=3kth ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Clp-family proteins are prototypes for studying the mechanism of ATP-dependent proteases because the proteolytic activity of the ClpP core is tightly regulated by activating Clp-ATPases. Nonetheless, the proteolytic activation mechanism has remained elusive because of the lack of a complex structure. Acyldepsipeptides (ADEPs), a recently discovered class of antibiotics, activate and disregulate ClpP. Here we have elucidated the structural changes underlying the ClpP activation process by ADEPs. We present the structures of Bacillus subtilis ClpP alone and in complex with ADEP1 and ADEP2. The structures show the closed-to-open-gate transition of the ClpP N-terminal segments upon activation as well as conformational changes restricted to the upper portion of ClpP. The direction of the conformational movement and the hydrophobic clustering that stabilizes the closed structure are markedly different from those of other ATP-dependent proteases, providing unprecedented insights into the activation of ClpP.
-===Structure of ClpP from Bacillus subtilis in orthorombic crystal form===
+Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism.,Lee BG, Park EY, Lee KE, Jeon H, Sung KH, Paulsen H, Rubsamen-Schaeff H, Brotz-Oesterhelt H, Song HK Nat Struct Mol Biol. 2010 Apr;17(4):471-8. Epub 2010 Mar 21. PMID:20305655<ref>PMID:20305655</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3kth" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-KTH is a 7 chains structure with sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KTH OCA].
+*[[Clp protease 3D structures|Clp protease 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bacillus subtilis]]
-[[Category: Endopeptidase Clp]]
+[[Category: Large Structures]]
-[[Category: Brotz-Oesterhelt, H.]]
+[[Category: Brotz-Oesterhelt H]]
-[[Category: Lee, B G.]]
+[[Category: Lee B-G]]
-[[Category: Song, H K.]]
+[[Category: Song HK]]
-[[Category: Atp-binding]]
-[[Category: Cytoplasm]]
-[[Category: Hydrolase]]
-[[Category: Nucleotide-binding]]
-[[Category: Protease]]
-[[Category: Serine protease]]
-[[Category: Stress response]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 24 09:03:16 2010''