1l05: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1l05.gif|left|200px]]<br /><applet load="1l05" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1l05, resolution 1.7&Aring;" />
-'''CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME'''<br />
-==Overview==
+==CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME==
-Measurements of changes in structure and stability caused by 13 different, substitutions for threonine 157 in phage T4 lysozyme show that the most, stable lysozyme variants contain hydrogen bonds analogous to those in the, wild-type enzyme and that structural adjustments allow the protein to be, surprisingly tolerant of amino-acid substitutions.
+<StructureSection load='1l05' size='340' side='right'caption='[[1l05]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1l05]] 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=1L05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L05 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]] 1.7&#8491;</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=1l05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l05 OCA], [https://pdbe.org/1l05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l05 RCSB], [https://www.ebi.ac.uk/pdbsum/1l05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l05 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/l0/1l05_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=1l05 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions.
-==About this Structure==
+Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.,Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW Nature. 1987 Nov 5-11;330(6143):41-6. PMID:3118211<ref>PMID:3118211</ref>
-L05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L05 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme., Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW, Nature. 1987 Nov 5-11;330(6143):41-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=3118211 3118211]
+</div>
-[[Category: Bacteriophage t4]]
+<div class="pdbe-citations 1l05" style="background-color:#fffaf0;"></div>
-[[Category: Lysozyme]]
-[[Category: Single protein]]
-[[Category: Alber, T.]]
-[[Category: Dao-Pin, S.]]
-[[Category: Matthews, B.W.]]
-[[Category: hydrolase (o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:06:59 2007''
+==See Also==
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia virus T4]]
+[[Category: Large Structures]]
+[[Category: Alber T]]
+[[Category: Dao-Pin S]]
+[[Category: Matthews BW]]