2zl2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "2zl2" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:2zl2.png|left|200px]]
+
==Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ==
 +
<StructureSection load='2zl2' size='340' side='right' caption='[[2zl2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2zl2]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZL2 FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
 +
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zl0|2zl0]], [[2zl3|2zl3]]</td></tr>
 +
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])</td></tr>
 +
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr>
 +
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zl2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zl2 RCSB], [http://www.ebi.ac.uk/pdbsum/2zl2 PDBsum]</span></td></tr>
 +
<table>
 +
== 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/zl/2zl2_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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
ClpP and its ATPase compartment, ClpX or ClpA, remove misfolded proteins in cells and are of utmost importance in protein quality control. The ring hexamers of ClpA or ClpX recognize, unfold, and translocate target substrates into the degradation chamber of the double-ring tetradecamer of ClpP. The overall reaction scheme catalyzed by ClpXP or ClpAP has been proposed; however, the molecular mechanisms associated with substrate recognition and degradation have not yet been clarified in detail. To investigate these mechanisms, we determined the crystal structures of ClpP from Helicobacter pylori in complex with product peptides bound to the active site as well as in the apo state. In the complex structure, the peptides are zipped with two antiparallel strands of ClpP and point to the adjacent active site, thus providing structural explanations for the broad substrate specificity, the product inhibition and the processive degradation of substrates in the chamber. The structures also suggest that substrate binding causes local conformational changes around the active site that ultimately induce the active conformation of ClpP.
-
{{STRUCTURE_2zl2| PDB=2zl2 | SCENE= }}
+
The structural basis for the activation and peptide recognition of bacterial ClpP.,Kim DY, Kim KK J Mol Biol. 2008 Jun 13;379(4):760-71. Epub 2008 Apr 20. PMID:18468623<ref>PMID:18468623</ref>
-
===Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_18468623}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[2zl2]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZL2 OCA].
+
</StructureSection>
-
 
+
-
==See Also==
+
-
*[[Clp Protease|Clp Protease]]
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:018468623</ref><references group="xtra"/>
+
[[Category: Endopeptidase Clp]]
[[Category: Endopeptidase Clp]]
[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]

Revision as of 09:13, 29 September 2014

Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ

2zl2, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2zl2"
Views
Personal tools
Navigation
Toolbox