1g07: Difference between revisions

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-[[Image:1g07.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149C==
-|PDB= 1g07 |SIZE=350|CAPTION= <scene name='initialview01'>1g07</scene>, resolution 1.7&Aring;
+<StructureSection load='1g07' size='340' side='right'caption='[[1g07]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=HED:2-HYDROXYETHYL DISULFIDE'>HED</scene>
+<table><tr><td colspan='2'>[[1g07]] 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=1G07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G07 FirstGlance]. <br>
-|ACTIVITY= [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]
+</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>
-|GENE=
+<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></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=1g07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g07 OCA], [https://pdbe.org/1g07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g07 RCSB], [https://www.ebi.ac.uk/pdbsum/1g07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g07 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/g0/1g07_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=1g07 ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF T4 LYSOZYME MUTANT V149C'''
+==See Also==
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
-==Overview==
+<references/>
-To investigate the structural and thermodynamic basis of the binding of solvent at internal sites within proteins a number of mutations were constructed in T4 lysozyme. Some of these were designed to introduce new solvent-binding sites. Others were intended to displace solvent from preexisting sites. In one case Val-149 was replaced with alanine, serine, cysteine, threonine, isoleucine, and glycine. Crystallographic analysis shows that, with the exception of isoleucine, each of these substitutions results in the binding of solvent at a polar site that is sterically blocked in the wild-type enzyme. Mutations designed to perturb or displace a solvent molecule present in the native enzyme included the replacement of Thr-152 with alanine, serine, cysteine, valine, and isoleucine. Although the solvent molecule was moved in some cases by up to 1.7 A, in no case was it completely removed from the folded protein. The results suggest that hydrogen bonds from the protein to bound solvent are energy neutral. The binding of solvent to internal sites within proteins also appears to be energy neutral except insofar as the bound solvent may prevent a loss of energy due to potential hydrogen bonding groups that would otherwise be unsatisfied. The introduction of a solvent-binding site appears to require not only a cavity to accommodate the water molecule but also the presence of polar groups to help satisfy its hydrogen-bonding potential. It may be easier to design a site to accommodate two or more water molecules rather than one as the solvent molecules can then hydrogen-bond to each other. For similar reasons it is often difficult to design a point mutation that will displace a single solvent molecule from the core of a protein.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia virus T4]]
-G07 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G07 OCA].
+[[Category: Large Structures]]
+[[Category: Baase WA]]
-==Reference==
+[[Category: Matthews BW]]
-Structural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme., Xu J, Baase WA, Quillin ML, Baldwin EP, Matthews BW, Protein Sci. 2001 May;10(5):1067-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11316887 11316887]
+[[Category: Quillin ML]]
-[[Category: Bacteriophage t4]]
+[[Category: Xu J]]
-[[Category: Lysozyme]]
-[[Category: Single protein]]
-[[Category: Baase, W A.]]
-[[Category: Matthews, B W.]]
-[[Category: Quillin, M L.]]
-[[Category: Xu, J.]]
-[[Category: CL]]
-[[Category: HED]]
-[[Category: bacteriolytic enzyme]]
-[[Category: glycosidase]]
-[[Category: hydrolase]]
-[[Category: o-glycosyl]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:18 2008''