1l30

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{{Seed}}
 
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[[Image:1l30.png|left|200px]]
 
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==REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY==
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The line below this paragraph, containing "STRUCTURE_1l30", creates the "Structure Box" on the page.
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<StructureSection load='1l30' size='340' side='right'caption='[[1l30]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1l30]] 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=1L30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L30 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]] 1.7&#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=1l30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l30 OCA], [https://pdbe.org/1l30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l30 RCSB], [https://www.ebi.ac.uk/pdbsum/1l30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l30 ProSAT]</span></td></tr>
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{{STRUCTURE_1l30| PDB=1l30 | SCENE= }}
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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/l3/1l30_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=1l30 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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To investigate the relation between protein stability and the predicted stabilities of individual secondary structural elements, residue Pro86 in an alpha-helix in phage T4 lysozyme was replaced by ten different amino acids. The x-ray crystal structures of seven of the mutant lysozymes were determined at high resolution. In each case, replacement of the proline resulted in the formation of an extended alpha-helix. This involves a large conformational change in residues 81 to 83 and smaller shifts that extend 20 angstroms across the protein surface. Unexpectedly, all ten amino acid substitutions marginally reduce protein thermostability. This insensitivity of stability to the amino acid at position 86 is not simply explained by statistical and thermodynamic criteria for helical propensity. The observed conformational changes illustrate a general mechanism by which proteins can tolerate mutations.
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===REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY===
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Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.,Alber T, Bell JA, Sun DP, Nicholson H, Wozniak JA, Cook S, Matthews BW Science. 1988 Feb 5;239(4840):631-5. PMID:3277275<ref>PMID:3277275</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1l30" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_3277275}}, adds the Publication Abstract to the page
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 3277275 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_3277275}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia virus T4]]
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1L30 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L30 OCA].
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[[Category: Large Structures]]
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[[Category: Bell JA]]
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==Reference==
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[[Category: Dao-Pin S]]
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Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability., Alber T, Bell JA, Sun DP, Nicholson H, Wozniak JA, Cook S, Matthews BW, Science. 1988 Feb 5;239(4840):631-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3277275 3277275]
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[[Category: Matthews BW]]
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[[Category: Enterobacteria phage t4]]
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Bell, J A.]]
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[[Category: Dao-Pin, S.]]
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[[Category: Matthews, B W.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:35:12 2008''
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Current revision

REPLACEMENTS OF PRO86 IN PHAGE T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY

PDB ID 1l30

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