2anx: Difference between revisions
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<StructureSection load='2anx' size='340' side='right' caption='[[2anx]], [[Resolution|resolution]] 1.04Å' scene=''> | <StructureSection load='2anx' size='340' side='right' caption='[[2anx]], [[Resolution|resolution]] 1.04Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2anx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2anx]] 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=2ANX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ANX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2anv|2anv]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2anv|2anv]]</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 | <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='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='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=2anx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2anx RCSB], [http://www.ebi.ac.uk/pdbsum/2anx PDBsum]</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=2anx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anx OCA], [http://pdbe.org/2anx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2anx RCSB], [http://www.ebi.ac.uk/pdbsum/2anx PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[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). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2anx" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bpp22]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Matthews, B W]] | [[Category: Matthews, B W]] | ||
Revision as of 02:03, 10 September 2015
crystal structure of bacteriophage P22 lysozyme mutant L87Mcrystal structure of bacteriophage P22 lysozyme mutant L87M
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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