1d9u: Difference between revisions

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 <StructureSection load='1d9u' size='340' side='right'caption='[[1d9u]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1d9u]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D9U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1d9u]] is a 2 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=1D9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D9U FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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]] 2.6&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1d9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9u OCA], [http://pdbe.org/1d9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d9u RCSB], [http://www.ebi.ac.uk/pdbsum/1d9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9u ProSAT]</span></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=1d9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d9u OCA], [https://pdbe.org/1d9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d9u RCSB], [https://www.ebi.ac.uk/pdbsum/1d9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d9u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LYS_LAMBD LYS_LAMBD]] Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Acts as a transglycosylase. Cleaves glycosidic bonds between the C1 of N-acetyl muramic acids (NAM) and C4 of N-acetyl glucosamines (NAG) of the peptidoglycan of the bacterial walls.
+[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1d9u ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The three-dimensional structure of the lytic transglycosylase from bacteriophage lambda, also known as bacteriophage lambda lysozyme, complexed to the hexasaccharide inhibitor, hexa-N-acetylchitohexaose, has been determined by X-ray crystallography at 2.6 A resolution. The unit cell contains two molecules of the lytic transglycosylase with two hexasaccharides bound. Each enzyme molecule is found to interact with four N-acetylglucosamine units from one hexasaccharide (subsites A-D) and two N-acetylglucosamine units from the second hexasaccharide (subsites E and F), resulting in all six subsites of the active site of this enzyme being filled. This crystallographic structure, therefore, represents the first example of a lysozyme in which all subsites are occupied, and detailed protein-oligosaccharide interactions are now available for this bacteriophage lytic transglycosylase. Examination of the active site furthermore reveals that of the two residues that have been implicated in the reaction mechanism of most other c-type lysozymes (Glu35 and Asp52 in hen egg white lysozyme), only a homologous Glu residue is present. The lambda lytic transglycosylase is therefore functionally closely related to the Escherichia coli Slt70 and Slt35 lytic transglycosylases and goose egg white lysozyme which also lack the catalytic aspartic acid.
-Crystal structure of the lytic transglycosylase from bacteriophage lambda in complex with hexa-N-acetylchitohexaose.,Leung AK, Duewel HS, Honek JF, Berghuis AM Biochemistry. 2001 May 15;40(19):5665-73. PMID:11341831<ref>PMID:11341831</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1d9u" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 27: @@
 __TOC__
 </StructureSection>
+[[Category: Escherichia virus Lambda]]
 [[Category: Large Structures]]
-[[Category: Lysozyme]]
+[[Category: Berghuis AM]]
-[[Category: Berghuis, A M]]
+[[Category: Duewel HS]]
-[[Category: Duewel, H S]]
+[[Category: Honek JF]]
-[[Category: Honek, J F]]
+[[Category: Leung AKW]]
-[[Category: Leung, A K.W]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Six-sugar complex]]
-[[Category: Transglycosylase]]