6d9i: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6d9i' size='340' side='right'caption='[[6d9i]], [[Resolution|resolution]] 1.15Å' scene=''> | <StructureSection load='6d9i' size='340' side='right'caption='[[6d9i]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6d9i]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6d9i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D9I FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6d9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d9i OCA], [https://pdbe.org/6d9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d9i RCSB], [https://www.ebi.ac.uk/pdbsum/6d9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d9i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/LYSC1_ANAPL LYSC1_ANAPL] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 28: | Line 28: | ||
[[Category: Anas platyrhynchos]] | [[Category: Anas platyrhynchos]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Christ D]] | |||
[[Category: Christ | [[Category: Langley DB]] | ||
[[Category: Langley | |||
Latest revision as of 18:20, 4 October 2023
Pekin duck egg lysozyme isoform II (DEL-II)Pekin duck egg lysozyme isoform II (DEL-II)
Structural highlights
FunctionLYSC1_ANAPL Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Publication Abstract from PubMedBACKGROUND: Lysozyme purified from duck eggs (DEL) has long been used as a model antigen as a counterpoint to the enzyme purified from hen eggs (HEL). However, unlike the single C-type variant found in hen eggs, duck eggs contain multiple isoforms: I, II and III. We recently reported the structures of isoforms I and III from Pekin duck (Anas platyrhynchos) and unequivocally determined the sequences of all three isoforms by mass spectrometry. Here we present the crystal structure of isoform II (DEL-II). RESULTS: Lysozyme isoform II was purified from isoforms I and III using ion-exchange and gel-filtration chromatography, then crystallized. X-ray diffraction data were collected to 1.15 A resolution and the structure of DEL-II was solved by molecular replacement using the structure of DEL-I as the search model. It contains two molecules in the crystallographic asymmetric unit: both molecules display a canonical C-type lysozyme fold and electron density consistent with the expected sequence. The most significant difference between the two molecules concerns different conformations of a surface loop containing one of the expected amino acid differences between the isoforms. CONCLUSIONS: The structure of DEL-II supports the primary sequence as elucidated by a combination of amino acid sequencing, DNA sequencing and mass spectrometry, with strong electron density confirming it to be an S37G G71R variant of DEL I, and differing from hen egg lysozyme at a total of 21 amino acid positions. Crystal structure of duck egg lysozyme isoform II (DEL-II).,Langley DB, Christ D BMC Struct Biol. 2018 Aug 22;18(1):10. doi: 10.1186/s12900-018-0090-7. PMID:30134879[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||