3dkt: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
==Crystal structure of Thermotoga maritima encapsulin== | ==Crystal structure of Thermotoga maritima encapsulin== | ||
<StructureSection load='3dkt' size='340' side='right' caption='[[3dkt]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='3dkt' size='340' side='right' caption='[[3dkt]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3dkt]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. The June 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Vaults'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_6 10.2210/rcsb_pdb/mom_2009_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DKT FirstGlance]. <br> | <table><tr><td colspan='2'>[[3dkt]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. The June 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Vaults'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_6 10.2210/rcsb_pdb/mom_2009_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DKT FirstGlance]. <br> | ||
</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=3dkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dkt OCA], [http://pdbe.org/3dkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dkt RCSB], [http://www.ebi.ac.uk/pdbsum/3dkt PDBsum]</span></td></tr> | </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=3dkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dkt OCA], [http://pdbe.org/3dkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dkt RCSB], [http://www.ebi.ac.uk/pdbsum/3dkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dkt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Line 11: | Line 12: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dk/3dkt_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dk/3dkt_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> |
Revision as of 12:20, 14 November 2018
Crystal structure of Thermotoga maritima encapsulinCrystal structure of Thermotoga maritima encapsulin
Structural highlights
Function[MARIT_THEMA] Protease that exhibits activity toward chymotrypsin and trypsin substrates. May have antibacterial activity. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCompartmentalization is an important organizational feature of life. It occurs at varying levels of complexity ranging from eukaryotic organelles and the bacterial microcompartments, to the molecular reaction chambers formed by enzyme assemblies. The structural basis of enzyme encapsulation in molecular compartments is poorly understood. Here we show, using X-ray crystallographic, biochemical and EM experiments, that a widespread family of conserved bacterial proteins, the linocin-like proteins, form large assemblies that function as a minimal compartment to package enzymes. We refer to this shell-forming protein as 'encapsulin'. The crystal structure of such a particle from Thermotoga maritima determined at 3.1-angstroms resolution reveals that 60 copies of the monomer assemble into a thin, icosahedral shell with a diameter of 240 angstroms. The interior of this nanocompartment is lined with conserved binding sites for short polypeptide tags present as C-terminal extensions of enzymes involved in oxidative-stress response. Structural basis of enzyme encapsulation into a bacterial nanocompartment.,Sutter M, Boehringer D, Gutmann S, Gunther S, Prangishvili D, Loessner MJ, Stetter KO, Weber-Ban E, Ban N Nat Struct Mol Biol. 2008 Sep;15(9):939-47. PMID:19172747[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
|