1ssy

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(New page: 200px<br /><applet load="1ssy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ssy, resolution 2.40&Aring;" /> '''Crystal structure of...)
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[[Image:1ssy.gif|left|200px]]<br /><applet load="1ssy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ssy, resolution 2.40&Aring;" />
 
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'''Crystal structure of phage T4 lysozyme mutant G28A/I29A/G30A/C54T/C97A'''<br />
 
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==Overview==
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==Crystal structure of phage T4 lysozyme mutant G28A/I29A/G30A/C54T/C97A==
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In general, alpha-helical conformations in proteins depend in large part, on the amino acid residues within the helix and their proximal, interactions. For example, an alanine residue has a high propensity to, adopt an alpha-helical conformation, whereas that of a glycine residue is, low. The sequence preferences for beta-sheet formation are less obvious., To identify the factors that influence beta-sheet conformation, a series, of scanning polyalanine mutations were made within the strands and, associated turns of the beta-sheet region in T4 lysozyme. For each, construct the stability of the folded protein was reduced substantially, consistent with removal of native packing interactions. However, the, crystal structures showed that each of the mutants retained the beta-sheet, conformation. These results suggest that the structure of the beta-sheet, region of T4 lysozyme is maintained to a substantial extent by tertiary, interactions with the surrounding parts of the protein. Such tertiary, interactions may be important in determining the structures of beta-sheets, in general.
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<StructureSection load='1ssy' size='340' side='right'caption='[[1ssy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ssy]] is a 2 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=1SSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SSY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ssy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssy OCA], [https://pdbe.org/1ssy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ssy RCSB], [https://www.ebi.ac.uk/pdbsum/1ssy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ssy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ss/1ssy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ssy ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1SSY 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=1SSY OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation., He MM, Wood ZA, Baase WA, Xiao H, Matthews BW, Protein Sci. 2004 Oct;13(10):2716-24. Epub 2004 Aug 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15340171 15340171]
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__TOC__
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[[Category: Bacteriophage t4]]
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</StructureSection>
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[[Category: Lysozyme]]
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[[Category: Escherichia virus T4]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baase, W.A.]]
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[[Category: Baase WA]]
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[[Category: He, M.M.]]
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[[Category: He MM]]
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[[Category: Heinz, D.W.]]
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[[Category: Heinz DW]]
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[[Category: Matthews, B.W.]]
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[[Category: Matthews BW]]
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[[Category: Xiao, H.]]
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[[Category: Xiao H]]
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[[Category: 3d-structure]]
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[[Category: bacteriolytic enzyme]]
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[[Category: glycosidase]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:38:19 2007''
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Current revision

Crystal structure of phage T4 lysozyme mutant G28A/I29A/G30A/C54T/C97A

PDB ID 1ssy

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