1l19: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1l19]] 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=1L19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L19 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1l19]] 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=1L19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L19 FirstGlance]. <br> | ||
</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=1l19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l19 OCA], [https://pdbe.org/1l19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l19 RCSB], [https://www.ebi.ac.uk/pdbsum/1l19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l19 ProSAT]</span></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]] 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=1l19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l19 OCA], [https://pdbe.org/1l19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l19 RCSB], [https://www.ebi.ac.uk/pdbsum/1l19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l19 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
Latest revision as of 11:44, 22 May 2024
ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLESENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES
Structural highlights
FunctionENLYS_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.[1] 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 PubMedTwo different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix. Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.,Nicholson H, Becktel WJ, Matthews BW Nature. 1988 Dec 15;336(6200):651-6. PMID:3200317[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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