1d9w
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1d9w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d9w, resolution 1.7Å" /> '''BACTERIOPHAGE T4 LYSO...) |
|||
| (17 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1d9w.jpg|left|200px]]<br /><applet load="1d9w" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1d9w, resolution 1.7Å" /> | ||
| - | '''BACTERIOPHAGE T4 LYSOZYME MUTANT'''<br /> | ||
| - | == | + | ==BACTERIOPHAGE T4 LYSOZYME MUTANT== |
| - | + | <StructureSection load='1d9w' size='340' side='right'caption='[[1d9w]], [[Resolution|resolution]] 1.91Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[1d9w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D9W 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]] 1.91Å</td></tr> |
| - | [ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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=1d9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9w OCA], [https://pdbe.org/1d9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d9w RCSB], [https://www.ebi.ac.uk/pdbsum/1d9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9w ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> |
| - | [ | + | == 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/d9/1d9w_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=1d9w ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia virus T4]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Korndoerfer IP]] | ||
| + | [[Category: Matthews BW]] | ||
Current revision
BACTERIOPHAGE T4 LYSOZYME MUTANT
| |||||||||||
