3hdf: Difference between revisions
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==Crystal structure of truncated endolysin R21 from phage 21== | |||
<StructureSection load='3hdf' size='340' side='right'caption='[[3hdf]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3hdf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_P21 Enterobacteria phage P21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HDF 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]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=3hdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hdf OCA], [https://pdbe.org/3hdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hdf RCSB], [https://www.ebi.ac.uk/pdbsum/3hdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hdf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ENLYS_BPP21 ENLYS_BPP21] Signal-arrest-release (SAR) endolysin with lysozyme activity that degrades host peptidoglycans and participates with the pinholin and spanin proteins in the sequential events which lead to programmed host cell lysis releasing the mature viral particles. Once the pinholin has permeabilized the host cell membrane, the SAR-endolysin is released into the periplasm where it breaks down the peptidoglycan layer.[HAMAP-Rule:MF_04136] | |||
== 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/hd/3hdf_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=3hdf ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
R(21), the lysozyme of coliphage 21, has an N-terminal signal-anchor-release (SAR) domain that directs its secretion in a membrane-tethered, inactive form and then its release and activation in the periplasm. Both genetic and crystallographic studies show that the SAR domain, once extracted from the bilayer, refolds into the body of the enzyme and effects muralytic activation by repositioning one residue of the canonical lysozyme catalytic triad. | |||
Regulation of a muralytic enzyme by dynamic membrane topology.,Sun Q, Kuty GF, Arockiasamy A, Xu M, Young R, Sacchettini JC Nat Struct Mol Biol. 2009 Nov;16(11):1192-4. Epub 2009 Nov 1. PMID:19881499<ref>PMID:19881499</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3hdf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterobacteria phage P21]] | |||
[[Category: Large Structures]] | |||
[[Category: Sacchettini JC]] | |||
[[Category: Sun Q]] | |||
Latest revision as of 08:52, 17 October 2024
Crystal structure of truncated endolysin R21 from phage 21Crystal structure of truncated endolysin R21 from phage 21
Structural highlights
FunctionENLYS_BPP21 Signal-arrest-release (SAR) endolysin with lysozyme activity that degrades host peptidoglycans and participates with the pinholin and spanin proteins in the sequential events which lead to programmed host cell lysis releasing the mature viral particles. Once the pinholin has permeabilized the host cell membrane, the SAR-endolysin is released into the periplasm where it breaks down the peptidoglycan layer.[HAMAP-Rule:MF_04136] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedR(21), the lysozyme of coliphage 21, has an N-terminal signal-anchor-release (SAR) domain that directs its secretion in a membrane-tethered, inactive form and then its release and activation in the periplasm. Both genetic and crystallographic studies show that the SAR domain, once extracted from the bilayer, refolds into the body of the enzyme and effects muralytic activation by repositioning one residue of the canonical lysozyme catalytic triad. Regulation of a muralytic enzyme by dynamic membrane topology.,Sun Q, Kuty GF, Arockiasamy A, Xu M, Young R, Sacchettini JC Nat Struct Mol Biol. 2009 Nov;16(11):1192-4. Epub 2009 Nov 1. PMID:19881499[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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