3hln: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{STRUCTURE_3hln|  PDB=3hln  |  SCENE=  }}
+==Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds==
-===Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds===
+<StructureSection load='3hln' size='340' side='right' caption='[[3hln]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-{{ABSTRACT_PUBMED_20637416}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3hln]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HLN FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0437, clpP, JW0427, lopP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+<tr id='activity'><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 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=3hln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hln OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hln RCSB], [http://www.ebi.ac.uk/pdbsum/3hln 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/hl/3hln_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 ==
+The highly conserved ClpP protease consists of two heptameric rings that interact by the interdigitation of an alpha-helix beta strand handle domain motif to form a tetradecameric cylinder. We previously proposed that protease dynamics results in the temporary unstructuring of interacting pairs of handle domains, opening transient equatorial side pores that allow for peptide egress. Here, we report the structure of an Escherichia coli ClpP mutant in which each opposing pair of protomers is linked by a disulfide bond. This structure resembles the compact structures of Streptococcus pneumoniae, Mycobacterium tuberculosis, and Plasmodium falciparum ClpPs, rather than the active, extended structures that have previously been determined for E. coli ClpPs. The structural data, along with normal mode analysis, support a model whereby the ClpP cylinder switches dynamically between an active extended state required for substrate degradation and an inactive compact state allowing peptide product release.
-==About this Structure==
+Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.,Kimber MS, Yu AY, Borg M, Leung E, Chan HS, Houry WA Structure. 2010 Jul 14;18(7):798-808. PMID:20637416<ref>PMID:20637416</ref>
-[[3hln]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HLN OCA].
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
 ==See Also==
 *[[Clp Protease|Clp Protease]]
 *[[Jmol/Visualizing large molecules|Jmol/Visualizing large molecules]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:020637416</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Endopeptidase Clp]]
 [[Category: Escherichia coli]]
-[[Category: Borg, M.]]
+[[Category: Borg, M]]
-[[Category: Chan, H S.]]
+[[Category: Chan, H S]]
-[[Category: Houry, W A.]]
+[[Category: Houry, W A]]
-[[Category: Kimber, M S.]]
+[[Category: Kimber, M S]]
-[[Category: Yu, A Y.H.]]
+[[Category: Yu, A Y.H]]
 [[Category: Atp-binding]]
 [[Category: Disordered equatorial loop]]