|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='3ab6' size='340' side='right'caption='[[3ab6]], [[Resolution|resolution]] 1.78Å' scene=''> | | <StructureSection load='3ab6' size='340' side='right'caption='[[3ab6]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ab6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Meretrix_lusoria Meretrix lusoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AB6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3AB6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ab6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meretrix_lusoria Meretrix lusoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AB6 FirstGlance]. <br> |
| - | </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></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]] 1.78Å</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=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene></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=3ab6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ab6 OCA], [http://pdbe.org/3ab6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ab6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ab6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ab6 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=3ab6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ab6 OCA], [https://pdbe.org/3ab6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ab6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ab6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ab6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LYS_MERLU LYS_MERLU]] Has antibacterial activity (By similarity).[UniProtKB:P83673] | + | [https://www.uniprot.org/uniprot/LYS_MERLU LYS_MERLU] Has antibacterial activity (By similarity).[UniProtKB:P83673] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 27: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]] | |
| | [[Category: Meretrix lusoria]] | | [[Category: Meretrix lusoria]] |
| - | [[Category: Araki, T]] | + | [[Category: Araki T]] |
| - | [[Category: Kuwano, Y]] | + | [[Category: Kuwano Y]] |
| - | [[Category: Yoneda, K]] | + | [[Category: Yoneda K]] |
| - | [[Category: Antibiotic]]
| + | |
| - | [[Category: Antimicrobial]]
| + | |
| - | [[Category: Bacteriolytic enzyme]]
| + | |
| - | [[Category: Glycosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Secreted]]
| + | |
| Structural highlights
Function
LYS_MERLU Has antibacterial activity (By similarity).[UniProtKB:P83673]
Publication Abstract from PubMed
To evaluate the structure-function relationships of invertebrate lysozymes, a new invertebrate-type (i-type) lysozyme was isolated from the common orient clam (Meretrix lusoria) and the tertiary structure of this enzyme was determined. Comparison of the tertiary structure of this enzyme with those of chicken and Venerupi philippinarum lysozymes revealed that the location of the side chain of the second catalytic residue, an aspartic acid, and the N-acetylglucosamine trimer bound at subsites A-C were different. Furthermore, the amino acid electrostatically interacting with Asp30 in V. philippinarum lysozyme, Lys108, was substituted by Gly in M. lusoria lysozyme and no other possible amino acid that could contribute to this interaction was found in M. lusoria lysozyme. It therefore seems that the substitutions of the amino acids at the interface of the V. philippinarum lysozyme dimer are likely to change the oligomeric state of the M. lusoria lysozyme.
The tertiary structure of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria).,Kuwano Y, Yoneda K, Kawaguchi Y, Araki T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1202-6. doi:, 10.1107/S1744309113028170. Epub 2013 Oct 26. PMID:24192349[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kuwano Y, Yoneda K, Kawaguchi Y, Araki T. The tertiary structure of an i-type lysozyme isolated from the common orient clam (Meretrix lusoria). Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1202-6. doi:, 10.1107/S1744309113028170. Epub 2013 Oct 26. PMID:24192349 doi:http://dx.doi.org/10.1107/S1744309113028170
|
