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3hdi
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3hdi.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of Bacillus halodurans metallo peptidase== |
| - | + | <StructureSection load='3hdi' size='340' side='right'caption='[[3hdi]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3hdi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HDI FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3hdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hdi OCA], [https://pdbe.org/3hdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hdi RCSB], [https://www.ebi.ac.uk/pdbsum/3hdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hdi ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9KA85_HALH5 Q9KA85_HALH5] | ||
| + | == 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/hd/3hdi_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=3hdi ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The M16 family of zinc peptidases comprises a pair of homologous domains that form two halves of a "clam-shell" surrounding the active site. The M16A and M16C subfamilies form one class ("peptidasomes"): they degrade 30-70 residue peptides, and adopt both open and closed conformations. The eukaryotic M16B subfamily forms a second class ("processing proteases"): they adopt a single partly-open conformation that enables them to cleave signal sequences from larger proteins. Here, we report the solution and crystal structures of a prokaryotic M16B peptidase, and demonstrate that it has features of both classes: thus, it forms stable "open" homodimers in solution that resemble the processing proteases; but the clam-shell closes upon binding substrate, a feature of the M16A/C peptidasomes. Moreover, clam-shell closure is required for proteolytic activity. We predict that other prokaryotic M16B family members will form dimeric peptidasomes, and propose a model for the evolution of the M16 family. | ||
| - | + | Crystal and solution structures of a prokaryotic M16B peptidase: an open and shut case.,Aleshin AE, Gramatikova S, Hura GL, Bobkov A, Strongin AY, Stec B, Tainer JA, Liddington RC, Smith JW Structure. 2009 Nov 11;17(11):1465-75. PMID:19913481<ref>PMID:19913481</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3hdi" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Alkalihalobacillus halodurans C-125]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Aleshin A]] | |
| - | == | + | [[Category: Gramatikova S]] |
| - | < | + | [[Category: Liddington RC]] |
| - | [[Category: | + | [[Category: Smith JW]] |
| - | [[Category: Aleshin | + | [[Category: Stec B]] |
| - | [[Category: Gramatikova | + | [[Category: Strongin AY]] |
| - | [[Category: Liddington | + | |
| - | [[Category: Smith | + | |
| - | [[Category: Stec | + | |
| - | [[Category: Strongin | + | |
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Current revision
Crystal structure of Bacillus halodurans metallo peptidase
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