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[[Image:1d3n.jpg|left|200px]]
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{{STRUCTURE_1d3n|  PDB=1d3n  |  SCENE=  }}
'''METHIONINE CORE MUTATION'''


==METHIONINE CORE MUTATION==
<StructureSection load='1d3n' size='340' side='right'caption='[[1d3n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d3n]] 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=1D3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D3N 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]] 2&#8491;</td></tr>
<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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1d3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3n OCA], [https://pdbe.org/1d3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d3n RCSB], [https://www.ebi.ac.uk/pdbsum/1d3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d3n 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/d3/1d3n_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1d3n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Using heavily methionine-substituted T4 lysozyme as an example, it is shown how the addition or deletion of a small number of methionines can simplify the location of selenium sites for use in MAD phasing. By comparing the X-ray data for a large number of singly substituted lysozymes, it is shown that the optimal amino acid to be substituted by methionine is leucine, followed, in order of preference, by phenylalanine, isoleucine and valine. The identification of leucine as the first choice agrees with the ranking suggested by the Dayhoff mutation probability, i.e. by the frequency of amino-acid substitutions in the sequences of related proteins. The ranking of the second and subsequent choices, however, differ significantly.


==Overview==
Use of differentially substituted selenomethionine proteins in X-ray structure determination.,Gassner NC, Matthews BW Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):1967-70. PMID:10666571<ref>PMID:10666571</ref>
Using heavily methionine-substituted T4 lysozyme as an example, it is shown how the addition or deletion of a small number of methionines can simplify the location of selenium sites for use in MAD phasing. By comparing the X-ray data for a large number of singly substituted lysozymes, it is shown that the optimal amino acid to be substituted by methionine is leucine, followed, in order of preference, by phenylalanine, isoleucine and valine. The identification of leucine as the first choice agrees with the ranking suggested by the Dayhoff mutation probability, i.e. by the frequency of amino-acid substitutions in the sequences of related proteins. The ranking of the second and subsequent choices, however, differ significantly.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1D3N 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=1D3N OCA].
</div>
<div class="pdbe-citations 1d3n" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Use of differentially substituted selenomethionine proteins in X-ray structure determination., Gassner NC, Matthews BW, Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):1967-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10666571 10666571]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
[[Category: Enterobacteria phage t4]]
== References ==
[[Category: Lysozyme]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Gassner, N C.]]
</StructureSection>
[[Category: Matthews, B W.]]
[[Category: Escherichia virus T4]]
[[Category: Methionine core mutant]]
[[Category: Large Structures]]
[[Category: Protein engineering]]
[[Category: Gassner NC]]
[[Category: Protein folding]]
[[Category: Matthews BW]]
[[Category: Selenomethionine]]
[[Category: T4 lysozyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:24:54 2008''

Latest revision as of 06:31, 30 October 2024

METHIONINE CORE MUTATION

1d3n, resolution 2.00Å

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