262l: Difference between revisions

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New page: left|200px<br /><applet load="262l" size="450" color="white" frame="true" align="right" spinBox="true" caption="262l, resolution 2.5Å" /> '''STRUCTURAL CHARACTERI...
 
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[[Image:262l.jpg|left|200px]]<br /><applet load="262l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="262l, resolution 2.5&Aring;" />
'''STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING'''<br />


==Overview==
==STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING==
To test a different approach to understanding the relationship between the, sequence of part of a protein and its conformation in the overall folded, structure, the amino acid sequence corresponding to an alpha-helix of T4, lysozyme was duplicated in tandem. The presence of such a sequence repeat, provides the protein with "choices" during folding. The mutant protein, folds with almost wild-type stability, is active, and crystallizes in two, different space groups, one isomorphous with wild type and the other with, two molecules in the asymmetric unit. The fold of the mutant is, essentially the same in all cases, showing that the inserted segment has a, well-defined structure. More than half of the inserted residues are, themselves helical and extend the helix present in the wild-type protein., Participation of additional duplicated residues in this helix would have, required major disruption of the parent structure. The results clearly, show that the residues within the duplicated sequence tend to maintain a, helical conformation even though the packing interactions with the, remainder of the protein are different from those of the original helix., It supports the hypothesis that the structures of individual alpha-helices, are determined predominantly by the nature of the amino acids within the, helix, rather than the structural environment provided by the rest of the, protein.
<StructureSection load='262l' size='340' side='right'caption='[[262l]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[262l]] 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=262L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=262L 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]] 2.5&#8491;</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=262l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=262l OCA], [https://pdbe.org/262l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=262l RCSB], [https://www.ebi.ac.uk/pdbsum/262l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=262l 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/62/262l_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=262l ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
262L 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=262L OCA].
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding., Sagermann M, Baase WA, Matthews BW, Proc Natl Acad Sci U S A. 1999 May 25;96(11):6078-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10339544 10339544]
__TOC__
[[Category: Bacteriophage t4]]
</StructureSection>
[[Category: Lysozyme]]
[[Category: Escherichia virus T4]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Baase, W.A.]]
[[Category: Baase WA]]
[[Category: Matthews, B.W.]]
[[Category: Matthews BW]]
[[Category: Sagermann, M.]]
[[Category: Sagermann M]]
[[Category: engineered tandem repeat]]
[[Category: hydrolase (o-glycosyl)]]
[[Category: protein design]]
[[Category: protein engineering]]
[[Category: t4 lysozyme]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:50:41 2007''

Latest revision as of 09:22, 3 April 2024

STRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDINGSTRUCTURAL CHARACTERISATION OF AN ENGINEERED TANDEM REPEAT CONTRASTS THE IMPORTANCE OF CONTEXT AND SEQUENCE IN PROTEIN FOLDING

Structural highlights

262l is a 2 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Moussa SH, Kuznetsov V, Tran TA, Sacchettini JC, Young R. Protein determinants of phage T4 lysis inhibition. Protein Sci. 2012 Apr;21(4):571-82. doi: 10.1002/pro.2042. Epub 2012 Mar 2. PMID:22389108 doi:http://dx.doi.org/10.1002/pro.2042

262l, resolution 2.50Å

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