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1l23
From Proteopedia
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==ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING== | ==ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING== | ||
| - | <StructureSection load='1l23' size='340' side='right' caption='[[1l23]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='1l23' size='340' side='right'caption='[[1l23]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1l23]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1l23]] 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=1L23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L23 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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=1l23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l23 OCA], [https://pdbe.org/1l23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l23 RCSB], [https://www.ebi.ac.uk/pdbsum/1l23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l23 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l2/1l23_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l2/1l23_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> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia virus T4]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Matthews | + | [[Category: Matthews BW]] |
| - | [[Category: Nicholson | + | [[Category: Nicholson H]] |
Current revision
ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
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