3ct5: Difference between revisions
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==Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail== | |||
<StructureSection load='3ct5' size='340' side='right'caption='[[3ct5]], [[Resolution|resolution]] 1.37Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ct5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CT5 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]] 1.37Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</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=3ct5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ct5 OCA], [https://pdbe.org/3ct5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ct5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ct5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ct5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GP13_BPPH2 GP13_BPPH2] May serve as a plug to restrain the highly pressurized packaged genome and thus would be the first virion protein to contact the host cell wall, degrading the peptidoglycan layer and thereby facilitating viral genome entry into the host bacteria. Acts probably as a multifunctional enzyme that degrades N-acetylglucosamine polymers (in vitro) and cleaves the peptide cross-links of the host cell wall. Essential for the tail assembly.<ref>PMID:18394643</ref> <ref>PMID:18606992</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/ct/3ct5_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=3ct5 ConSurf]. | |||
<div style="clear:both"></div> | |||
== | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus phage phi29]] | [[Category: Bacillus phage phi29]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Rossmann | [[Category: Rossmann MG]] | ||
[[Category: Xiang | [[Category: Xiang Y]] | ||
Latest revision as of 12:38, 21 February 2024
Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tailCrystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail
Structural highlights
FunctionGP13_BPPH2 May serve as a plug to restrain the highly pressurized packaged genome and thus would be the first virion protein to contact the host cell wall, degrading the peptidoglycan layer and thereby facilitating viral genome entry into the host bacteria. Acts probably as a multifunctional enzyme that degrades N-acetylglucosamine polymers (in vitro) and cleaves the peptide cross-links of the host cell wall. Essential for the tail assembly.[1] [2] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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