1cx6
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1cx6' size='340' side='right'caption='[[1cx6]], [[Resolution|resolution]] 2.01Å' scene=''> | <StructureSection load='1cx6' size='340' side='right'caption='[[1cx6]], [[Resolution|resolution]] 2.01Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1cx6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1cx6]] 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=1CX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CX6 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]] 2.01Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1cx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cx6 OCA], [https://pdbe.org/1cx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cx6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cx6 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=1cx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cx6 OCA], [https://pdbe.org/1cx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cx6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cx6 ProSAT]</span></td></tr> | ||
</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]] | ||
| Line 22: | Line 20: | ||
</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=1cx6 ConSurf]. | </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=1cx6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The availability of a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has made it possible to systematically compare the effect on protein stability of selenomethionine relative to methionine. Wild-type lysozyme contains two fully buried methionine residues plus three more on the surface. The substitution of these methionine residues with selenomethionine slightly stabilizes the protein. As more and more methionine residues are substituted into the protein, there is a progressive loss of stability. This is, however, increasingly offset in the selenomethionine variants, ultimately resulting in a differential increase in melting temperature of about 7 degrees C. This increase, corresponding to about 0.25 kcal/mol per substitution, is in reasonable agreement with the difference in the solvent transfer free energy between the two amino acids. | ||
| - | |||
| - | Substitution with selenomethionine can enhance the stability of methionine-rich proteins.,Gassner NC, Baase WA, Hausrath AC, Matthews BW J Mol Biol. 1999 Nov 19;294(1):17-20. PMID:10556025<ref>PMID:10556025</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1cx6" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 38: | Line 27: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia virus T4]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Baase WA]] | |
| - | [[Category: Baase | + | [[Category: Gassner NC]] |
| - | [[Category: Gassner | + | [[Category: Matthews BW]] |
| - | [[Category: Matthews | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Revision as of 15:44, 13 March 2024
T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE
| |||||||||||
