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==crystal structure of P22 lysozyme mutant L86M==
==crystal structure of P22 lysozyme mutant L86M==
<StructureSection load='2anv' size='340' side='right' caption='[[2anv]], [[Resolution|resolution]] 1.04&Aring;' scene=''>
<StructureSection load='2anv' size='340' side='right'caption='[[2anv]], [[Resolution|resolution]] 1.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2anv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANV FirstGlance]. <br>
<table><tr><td colspan='2'>[[2anv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ANV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.04&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2anx|2anx]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">19 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 BPP22])</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=2anv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anv OCA], [https://pdbe.org/2anv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2anv RCSB], [https://www.ebi.ac.uk/pdbsum/2anv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2anv ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2anv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anv OCA], [http://pdbe.org/2anv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2anv RCSB], [http://www.ebi.ac.uk/pdbsum/2anv PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ENLYS_BPP22 ENLYS_BPP22]] Endolysin with lysozyme 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 (By similarity).  
[https://www.uniprot.org/uniprot/ENLYS_BPP22 ENLYS_BPP22] Endolysin with lysozyme 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 (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/2anv_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/2anv_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2anv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The X-ray crystal structure of the previously unknown bacteriophage P22 lysozyme, the product of gene 19, has been determined ab initio by direct methods using the program SIR2002. The presence of several partially occupied iodine anions and samarium cations augmented the ability of direct methods to locate all 2268 non-H protein atoms in the asymmetric unit, making this one of the largest structures to date to be determined ab initio. The iodides were introduced from a quick soak, which the crystal survived sufficiently well to diffract to 1.04 angstroms resolution. The complete heavy-atom substructure contributed 6.6% of the total scattering power. The initial determination of the structure assumed that there were two iodide ions in the asymmetric unit, although it was later determined that these sites correspond to partially occupied samarium ions. Tests suggested that it is better to overestimate rather than underestimate the heavy-atom content. While experimental phases from all of the successful tests were of high quality, the best results came from a SAD experiment using the programs SHELXD and SHELXE. Nonetheless, ab initio structure determination by direct methods was found to be a viable alternative to traditional protein crystallographic methods provided that the X-ray data extend to atomic resolution and heavy atoms with sufficient scattering power are present in the crystal.
Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme.,Mooers BH, Matthews BW Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):165-76. Epub 2006, Jan 18. PMID:16421448<ref>PMID:16421448</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2anv" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
*[[NADP-dependent malic enzyme|NADP-dependent malic enzyme]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpp22]]
[[Category: Large Structures]]
[[Category: Lysozyme]]
[[Category: Salmonella virus P22]]
[[Category: Matthews, B W]]
[[Category: Matthews BW]]
[[Category: Mooers, B H]]
[[Category: Mooers BH]]
[[Category: Direct method]]
[[Category: Hydrolase]]
[[Category: Lanthinide binding site]]
[[Category: Phage lysozyme]]
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