1am7

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(New page: 200px<br /> <applet load="1am7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1am7, resolution 2.3&Aring;" /> '''LYSOZYME FROM BACTER...)
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[[Image:1am7.gif|left|200px]]<br />
 
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<applet load="1am7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1am7, resolution 2.3&Aring;" />
 
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'''LYSOZYME FROM BACTERIOPHAGE LAMBDA'''<br />
 
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==Overview==
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==Lysozyme from bacteriophage lambda==
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Like other lysozymes, the bacteriophage lambda lysozyme is involved in the, digestion of bacterial walls. This enzyme is remarkable in that its, mechanism of action is different from the classical lysozyme's mechanism., From the point of view of protein evolution, it shows features of, lysozymes from different classes. The crystal structure of the enzyme in, which all tryptophan residues have been replaced by aza-tryptophan has, been solved by X-ray crystallography at 2.3 A using a combination of, multiple isomorphous replacement, non-crystallographic symmetry averaging, and density modification techniques. There are three molecules in the, asymmetric unit. The characteristic structural elements of lysozymes are, conserved: each molecule is organized in two domains connected by a helix, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9514719 (full description)]]
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<StructureSection load='1am7' size='340' side='right'caption='[[1am7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1am7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AM7 FirstGlance]. <br>
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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]] 2.3&#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=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=TRN:NZ2-TRYPTOPHAN'>TRN</scene></td></tr>
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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=1am7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1am7 OCA], [https://pdbe.org/1am7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1am7 RCSB], [https://www.ebi.ac.uk/pdbsum/1am7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1am7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ENLYS_LAMBD ENLYS_LAMBD] Endolysin with transglycosylase 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.[HAMAP-Rule:MF_04109]<ref>PMID:10556513</ref> <ref>PMID:24113139</ref>
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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/am/1am7_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=1am7 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1AM7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]] with IPA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AM7 OCA]].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==Reference==
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<references/>
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Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes., Evrard C, Fastrez J, Declercq JP, J Mol Biol. 1998 Feb 13;276(1):151-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9514719 9514719]
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__TOC__
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[[Category: Bacteriophage lambda]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Escherichia virus Lambda]]
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[[Category: Declercq, J.P.]]
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[[Category: Large Structures]]
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[[Category: Evrard, C.]]
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[[Category: Declercq JP]]
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[[Category: Fastrez, J.]]
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[[Category: Evrard C]]
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[[Category: IPA]]
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[[Category: Fastrez J]]
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[[Category: evolution]]
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[[Category: glycosidase]]
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[[Category: lysozyme]]
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[[Category: transglycosylase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:31:31 2007''
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Current revision

Lysozyme from bacteriophage lambda

PDB ID 1am7

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