1l18

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<StructureSection load='1l18' size='340' side='right'caption='[[1l18]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1l18' size='340' side='right'caption='[[1l18]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1l18]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L18 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1l18]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L18 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2lzm|2lzm]], [[1l01|1l01]], [[1l02|1l02]], [[1l03|1l03]], [[1l04|1l04]], [[1l05|1l05]], [[1l06|1l06]], [[1l07|1l07]], [[1l08|1l08]], [[1l09|1l09]], [[1l10|1l10]], [[1l11|1l11]], [[1l12|1l12]], [[1l13|1l13]], [[1l14|1l14]], [[1l15|1l15]], [[1l16|1l16]], [[1l17|1l17]], [[1l19|1l19]], [[1l20|1l20]], [[1l21|1l21]], [[1l22|1l22]], [[1l23|1l23]], [[1l24|1l24]], [[1l25|1l25]], [[1l26|1l26]], [[1l27|1l27]], [[1l28|1l28]], [[1l29|1l29]], [[1l30|1l30]], [[1l31|1l31]], [[1l32|1l32]], [[1l33|1l33]], [[1l34|1l34]], [[1l35|1l35]], [[1l36|1l36]]</div></td></tr>
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</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=1l18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l18 OCA], [https://pdbe.org/1l18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l18 RCSB], [https://www.ebi.ac.uk/pdbsum/1l18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l18 ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></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=1l18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l18 OCA], [https://pdbe.org/1l18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l18 RCSB], [https://www.ebi.ac.uk/pdbsum/1l18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l18 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/LYS_BPT4 LYS_BPT4]] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.
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[https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] 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.<ref>PMID:22389108</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpt4]]
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[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lysozyme]]
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[[Category: Dao-Pin S]]
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[[Category: Dao-Pin, S]]
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[[Category: Matsumura M]]
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[[Category: Matsumura, M]]
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[[Category: Matthews BW]]
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[[Category: Matthews, B W]]
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Revision as of 10:17, 24 November 2022

HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3

PDB ID 1l18

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