|
|
| Line 3: |
Line 3: |
| <StructureSection load='1am7' size='340' side='right'caption='[[1am7]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1am7' size='340' side='right'caption='[[1am7]], [[Resolution|resolution]] 2.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1am7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage 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 [http://proteopedia.org/fgij/fg.htm?mol=1AM7 FirstGlance]. <br> | | <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> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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]] 2.3Å</td></tr> |
| <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRN:NZ2-TRYPTOPHAN'>TRN</scene></td></tr> | | <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> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</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=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> |
| <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://proteopedia.org/fgij/fg.htm?mol=1am7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1am7 OCA], [http://pdbe.org/1am7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1am7 RCSB], [http://www.ebi.ac.uk/pdbsum/1am7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1am7 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == 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 == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 22: |
Line 20: |
| </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]. | | </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]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| 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 and the essential catalytic residue (Glu19) is located in the depth of a cleft between the two domains. This cleft shows an open conformation in two of the independent molecules, while access to the cavity is much more restricted in the last one. A structural alignment with T4 lysozyme and hen egg white lysozyme allows us to superpose about 60 C alpha atoms with a rms distance close to 2 A. The best alignments concern the helix preceding the catalytic residue, some parts of the beta sheets and the helix joining the two domains. The results of sequence alignments with the V and C lysozymes, in which weak local similarities had been detected, are compared with the structural results.
| |
|
| |
| 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:9514719<ref>PMID:9514719</ref>
| |
|
| |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 1am7" style="background-color:#fffaf0;"></div>
| |
|
| |
|
| ==See Also== | | ==See Also== |
| Line 38: |
Line 27: |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacteriophage lambda]] | | [[Category: Escherichia virus Lambda]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Lysozyme]]
| | [[Category: Declercq JP]] |
| [[Category: Declercq, J P]] | | [[Category: Evrard C]] |
| [[Category: Evrard, C]] | | [[Category: Fastrez J]] |
| [[Category: Fastrez, J]] | |
| [[Category: Evolution]]
| |
| [[Category: Glycosidase]]
| |
| [[Category: Transglycosylase]]
| |