1m4y: Difference between revisions

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 <StructureSection load='1m4y' size='340' side='right'caption='[[1m4y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1m4y]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M4Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1m4y]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M4Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ned|1ned]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1m4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4y OCA], [http://pdbe.org/1m4y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m4y RCSB], [http://www.ebi.ac.uk/pdbsum/1m4y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4y ProSAT]</span></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=1m4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4y OCA], [https://pdbe.org/1m4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m4y RCSB], [https://www.ebi.ac.uk/pdbsum/1m4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4y ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HSLV_THEMA HSLV_THEMA]] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.<ref>PMID:12646382</ref>
+[https://www.uniprot.org/uniprot/HSLV_THEMA HSLV_THEMA] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.<ref>PMID:12646382</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1m4y ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Heat-shock locus VU (HslVU) is an ATP-dependent proteolytic system and a prokaryotic homolog of the proteasome. It consists of HslV, the protease, and HslU, the ATPase and chaperone. We have cloned, sequenced and expressed both protein components from the hyperthermophile Thermotoga maritima. T. maritima HslU hydrolyzes a variety of nucleotides in a temperature-dependent manner, with the optimum lying between 75 and 80 degrees C. It is also nucleotide-unspecific for activation of HslV against amidolytic and caseinolytic activity. The Escherichia coli and T. maritima HslU proteins mutually stimulate HslV proteins from both sources, suggesting a conserved activation mechanism. The crystal structure of T. maritima HslV was determined and refined to 2.1-A resolution. The structure of the dodecameric enzyme is well conserved compared to those from E. coli and Haemophilus influenzae. A comparison of known HslV structures confirms the presence of a cation-binding site, although its exact role in the proteolytic mechanism of HslV remains unclear. Amongst factors responsible for the thermostability of T. maritima HslV, extensive ionic interactions/salt-bridge networks, which occur specifically in the T. maritima enzyme in comparison to its mesophilic counterparts, seem to play an important role.
-Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV.,Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R Biophys Chem. 2003;100(1-3):437-52. PMID:12646382<ref>PMID:12646382</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1m4y" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 43589]]
 [[Category: Large Structures]]
-[[Category: Azim, M K]]
+[[Category: Thermotoga maritima]]
-[[Category: Bochtler, M B]]
+[[Category: Azim MK]]
-[[Category: Hartmann, C]]
+[[Category: Bochtler MB]]
-[[Category: Huber, R]]
+[[Category: Hartmann C]]
-[[Category: Ramachandran, R]]
+[[Category: Huber R]]
-[[Category: Song, H K]]
+[[Category: Ramachandran R]]
-[[Category: Hydrolase]]
+[[Category: Song HK]]
-[[Category: N-terminal catalytic threonine residue]]