7yrk: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7yrk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YRK FirstGlance]. <br> | <table><tr><td colspan='2'>[[7yrk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YRK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=74C:methyl+radical'>74C</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=JI6:(6~{S})-6-[(1~{R})-1-oxidanylethyl]-2,4-dioxa-7$l^{4}-aza-3$l^{3}-cupratricyclo[7.4.0.0^{3,7}]trideca-1(13),7,9,11-tetraen-5-one'>JI6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 0.92Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=74C:methyl+radical'>74C</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=JI6:(6~{S})-6-[(1~{R})-1-oxidanylethyl]-2,4-dioxa-7$l^{4}-aza-3$l^{3}-cupratricyclo[7.4.0.0^{3,7}]trideca-1(13),7,9,11-tetraen-5-one'>JI6</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=7yrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yrk OCA], [https://pdbe.org/7yrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yrk RCSB], [https://www.ebi.ac.uk/pdbsum/7yrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yrk 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=7yrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yrk OCA], [https://pdbe.org/7yrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yrk RCSB], [https://www.ebi.ac.uk/pdbsum/7yrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yrk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 7yrk" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7yrk" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 21:11, 29 November 2023
Crystal structure of the hen egg lysozyme-2-oxidobenzylidene-threoninato-copper (II) complexCrystal structure of the hen egg lysozyme-2-oxidobenzylidene-threoninato-copper (II) complex
Structural highlights
FunctionLYSC_CHICK 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. Has bacteriolytic activity against M.luteus.[1] Publication Abstract from PubMedA novel hybrid protein composed of a superoxide dismutase-active Cu(II) complex (CuST) and lysozyme (CuST@lysozyme) was prepared. The results of the spectroscopic and electrochemical analyses confirmed that CuST binds to lysozyme. We determined the crystal structure of CuST@lysozyme at 0.92 A resolution, which revealed that the His15 imidazole group of lysozyme binds to the Cu(II) center of CuST in the equatorial position. In addition, CuST was fixed in position by the weak axial coordination of the Thr89 hydroxyl group and the hydrogen bond between the guanidinium group of the Arg14 residue and the hydroxyl group of CuST. Furthermore, the combination of CuST with lysozyme did not decrease the superoxide dismutase activity of CuST. Based on the spectral, electrochemical, structural studies, and quantum chemical calculations, an O(2)(-) disproportionation mechanism catalyzed by CuST@lysozyme is proposed. A novel hybrid protein composed of superoxide-dismutase-active Cu(II) complex and lysozyme.,Furuya T, Nakane D, Kitanishi K, Katsuumi N, Tsaturyan A, Shcherbakov IN, Unno M, Akitsu T Sci Rep. 2023 Apr 27;13(1):6892. doi: 10.1038/s41598-023-33926-1. PMID:37106030[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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