3ab6: Difference between revisions
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==Crystal structure of NAG3 bound lysozyme from Meretrix lusoria== | |||
<StructureSection load='3ab6' size='340' side='right'caption='[[3ab6]], [[Resolution|resolution]] 1.78Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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'>[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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LYS_MERLU LYS_MERLU] Has antibacterial activity (By similarity).[UniProtKB:P83673] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24192349</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ab6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Meretrix lusoria]] | |||
[[Category: Araki T]] | |||
[[Category: Kuwano Y]] | |||
[[Category: Yoneda K]] | |||
Latest revision as of 17:17, 1 November 2023
Crystal structure of NAG3 bound lysozyme from Meretrix lusoriaCrystal structure of NAG3 bound lysozyme from Meretrix lusoria
Structural highlights
FunctionLYS_MERLU Has antibacterial activity (By similarity).[UniProtKB:P83673] Publication Abstract from PubMedTo 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 AlsoReferences
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