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1yb0

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[[Image:1yb0.gif|left|200px]]<br /><applet load="1yb0" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yb0, resolution 1.86&Aring;" />
 
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'''Structure of PlyL'''<br />
 
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==Overview==
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==Structure of PlyL==
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We report a structural and functional analysis of the lambda prophage Ba02 endolysin (PlyL) encoded by the Bacillus anthracis genome. We show that PlyL comprises two autonomously folded domains, an N-terminal catalytic domain and a C-terminal cell wall-binding domain. We determined the crystal structure of the catalytic domain; its three-dimensional fold is related to that of the cell wall amidase, T7 lysozyme, and contains a conserved zinc coordination site and other components of the catalytic machinery. We demonstrate that PlyL is an N-acetylmuramoyl-L-alanine amidase that cleaves the cell wall of several Bacillus species when applied exogenously. We show, unexpectedly, that the catalytic domain of PlyL cleaves more efficiently than the full-length protein, except in the case of Bacillus cereus, and using GFP-tagged cell wall-binding domain, we detected strong binding of the cell wall-binding domain to B. cereus but not to other species tested. We further show that a related endolysin (Ply21) from the B. cereus phage, TP21, shows a similar pattern of behavior. To explain these data, and the species specificity of PlyL, we propose that the C-terminal domain inhibits the activity of the catalytic domain through intramolecular interactions that are relieved upon binding of the C-terminal domain to the cell wall. Furthermore, our data show that (when applied exogenously) targeting of the enzyme to the cell wall is not a prerequisite of its lytic activity, which is inherently high. These results may have broad implications for the design of endolysins as therapeutic agents.
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<StructureSection load='1yb0' size='340' side='right'caption='[[1yb0]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1yb0]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YB0 FirstGlance]. <br>
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1YB0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YB0 OCA].
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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]] 1.86&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==Reference==
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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=1yb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yb0 OCA], [https://pdbe.org/1yb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yb0 RCSB], [https://www.ebi.ac.uk/pdbsum/1yb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yb0 ProSAT]</span></td></tr>
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Structure and lytic activity of a Bacillus anthracis prophage endolysin., Low LY, Yang C, Perego M, Osterman A, Liddington RC, J Biol Chem. 2005 Oct 21;280(42):35433-9. Epub 2005 Aug 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16103125 16103125]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A6H3AMF3_BACAN A0A6H3AMF3_BACAN]
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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/yb/1yb0_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=1yb0 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bacillus anthracis]]
[[Category: Bacillus anthracis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Liddington, R C.]]
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[[Category: Liddington RC]]
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[[Category: Low, L Y.]]
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[[Category: Low LY]]
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[[Category: Osterman, A.]]
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[[Category: Osterman A]]
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[[Category: Perego, M.]]
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[[Category: Perego M]]
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[[Category: Yang, C.]]
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[[Category: Yang C]]
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[[Category: PO4]]
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[[Category: ZN]]
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[[Category: e c.3 5.1 28]]
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[[Category: n-acetylmuramoyl-l-alanine amidase]]
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[[Category: plyl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:03:30 2008''
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Current revision

Structure of PlyL

PDB ID 1yb0

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