1yb0

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(New page: 200px<br /><applet load="1yb0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yb0, resolution 1.86&Aring;" /> '''Structure of PlyL'''...)
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[[Image:1yb0.gif|left|200px]]<br /><applet load="1yb0" size="450" 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 ZN and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.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://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:51:28 2007''
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Current revision

Structure of PlyL

PDB ID 1yb0

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