182l: Difference between revisions

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-[[Image:182l.gif|left|200px]]<br /><applet load="182l" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="182l, resolution 1.80&Aring;" />
-'''SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY'''<br />
-==Overview==
+==SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY==
-To better understand the role of shape complementarity in ligand binding, and protein core interactions, the structures have been determined of a, set of ligands bound within a cavity-containing mutant of T4 lysozyme. The, interior cavity is seen to consist of two parts that respond very, differently to the binding of ligands. First, there is a relatively rigid, region that does not relax significantly upon binding any ligand. Second, there is a more flexible region that moves to various extents in response, to binding the different ligands. The part of the binding site that, remains rigid is characterized by low temperature factors and strong, protection from hydrogen exchange. This part of the site appears to be, primarily responsible for discriminating between ligands of different, shape (i.e., for determining specificity). The more flexible region, characterized by relatively high temperature factors and weak protection, from hydrogen exchange, allows some promiscuity in binding by undergoing, variable amounts of deformation at essentially the same energetic cost., This linkage between the dynamic information represented by, crystallographic temperature factors and hydrogen-exchange behavior on the, one hand, and structural plasticity in response to ligand binding on the, other hand, suggests a way to improve our understanding of steric, interactions in protein cores and protein-ligand binding sites. Ligand, design and packing algorithms might take advantage of this information, requiring complementary interactions where the protein is rigid and, allowing some overlap in regions where the protein is flexible.
+<StructureSection load='182l' size='340' side='right'caption='[[182l]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[182l]] 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=182L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=182L 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]] 1.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BZF:BENZOFURAN'>BZF</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</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=182l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=182l OCA], [https://pdbe.org/182l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=182l RCSB], [https://www.ebi.ac.uk/pdbsum/182l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=182l 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/82/182l_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=182l ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2] with CL, HED and BZF as [http://en.wikipedia.org/wiki/ligands ligands]. 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=182L OCA].
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
-==Reference==
+<references/>
-Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity., Morton A, Matthews BW, Biochemistry. 1995 Jul 11;34(27):8576-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7612599 7612599]
+__TOC__
-[[Category: Enterobacteria phage t2]]
+</StructureSection>
-[[Category: Lysozyme]]
+[[Category: Escherichia virus T4]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Matthews, B.W.]]
+[[Category: Matthews BW]]
-[[Category: Morton, A.]]
+[[Category: Morton A]]
-[[Category: BZF]]
-[[Category: CL]]
-[[Category: HED]]
-[[Category: hydrolase (o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:30:16 2007''