4hpi: Difference between revisions
New page: '''Unreleased structure''' The entry 4hpi is ON HOLD Authors: Naoyuki, U., Tomoyuki, N., Takayuki, O., Tamo, F. Description: Crystal Structure of Hen Egg White Lysozyme complex with GN... |
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==Crystal Structure of Hen Egg White Lysozyme complex with GN2-M== | |||
<StructureSection load='4hpi' size='340' side='right'caption='[[4hpi]], [[Resolution|resolution]] 1.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hpi]] 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=4HPI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HPI 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]] 1.19Å</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=4hpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hpi OCA], [https://pdbe.org/4hpi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hpi RCSB], [https://www.ebi.ac.uk/pdbsum/4hpi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hpi ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_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.<ref>PMID:22044478</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
4-O-beta-Di-N-acetylchitobiosyl moranoline (2) and 4-O-beta-tri-N-acetylchitotriosyl moranoline (3) were produced by lysozyme-mediated transglycosylation from the substrates tetra-N-acetylchitotetraose, (GlcNAc)4, and moranoline, and the binding modes of 2 and 3 to hen egg white lysozyme (HEWL) was examined by inhibition kinetics, isothermal titration calorimetry (ITC), and x-ray crystallography. Compounds 2 and 3 specifically bound to HEWL, acting as competitive inhibitors with Ki values of 2.01 x 10(-5) and 1.84 x 10(-6) m, respectively. From ITC analysis, the binding of 3 was found to be driven by favorable enthalpy change (DeltaHr degrees ), which is similar to those obtained for 2 and (GlcNAc)4. However, the entropy loss (-TDeltaSr degrees ) for the binding of 3 was smaller than those of 2 and (GlcNAc)4. Thus the binding of 3 was found to be more favorable than those of the others. Judging from the Kd value of 3 (760 nm), the compound appears to have the highest affinity among the lysozyme inhibitors identified to date. X-ray crystal structure of HEWL in a complex with 3 showed that compound 3 binds to subsites -4 to -1 and the moranoline moiety adopts an undistorted (4)C1 chair conformation almost overlapping with the -1 sugar covalently bound to Asp-52 of HEWL (Vocadlo, Davies, G. J., Laine, R., and Withers, S. G. (2001) Nature 412, 835-838). From these results, we concluded that compound 3 serves as a transition-state analogue for lysozyme providing additional evidence supporting the covalent glycosyl-enzyme intermediate in the catalytic reaction. | |||
A novel transition-state analogue for lysozyme, 4-O-beta-tri-N-acetylchitotriosyl moranoline, provided evidence supporting the covalent glycosyl-enzyme intermediate.,Ogata M, Umemoto N, Ohnuma T, Numata T, Suzuki A, Usui T, Fukamizo T J Biol Chem. 2013 Mar 1;288(9):6072-82. doi: 10.1074/jbc.M112.439281. Epub 2013, Jan 9. PMID:23303182<ref>PMID:23303182</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hpi" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Fukamizo T]] | |||
[[Category: Numata T]] | |||
[[Category: Ohnuma T]] | |||
[[Category: Umemoto N]] | |||
Latest revision as of 09:15, 11 September 2024
Crystal Structure of Hen Egg White Lysozyme complex with GN2-MCrystal Structure of Hen Egg White Lysozyme complex with GN2-M
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 PubMed4-O-beta-Di-N-acetylchitobiosyl moranoline (2) and 4-O-beta-tri-N-acetylchitotriosyl moranoline (3) were produced by lysozyme-mediated transglycosylation from the substrates tetra-N-acetylchitotetraose, (GlcNAc)4, and moranoline, and the binding modes of 2 and 3 to hen egg white lysozyme (HEWL) was examined by inhibition kinetics, isothermal titration calorimetry (ITC), and x-ray crystallography. Compounds 2 and 3 specifically bound to HEWL, acting as competitive inhibitors with Ki values of 2.01 x 10(-5) and 1.84 x 10(-6) m, respectively. From ITC analysis, the binding of 3 was found to be driven by favorable enthalpy change (DeltaHr degrees ), which is similar to those obtained for 2 and (GlcNAc)4. However, the entropy loss (-TDeltaSr degrees ) for the binding of 3 was smaller than those of 2 and (GlcNAc)4. Thus the binding of 3 was found to be more favorable than those of the others. Judging from the Kd value of 3 (760 nm), the compound appears to have the highest affinity among the lysozyme inhibitors identified to date. X-ray crystal structure of HEWL in a complex with 3 showed that compound 3 binds to subsites -4 to -1 and the moranoline moiety adopts an undistorted (4)C1 chair conformation almost overlapping with the -1 sugar covalently bound to Asp-52 of HEWL (Vocadlo, Davies, G. J., Laine, R., and Withers, S. G. (2001) Nature 412, 835-838). From these results, we concluded that compound 3 serves as a transition-state analogue for lysozyme providing additional evidence supporting the covalent glycosyl-enzyme intermediate in the catalytic reaction. A novel transition-state analogue for lysozyme, 4-O-beta-tri-N-acetylchitotriosyl moranoline, provided evidence supporting the covalent glycosyl-enzyme intermediate.,Ogata M, Umemoto N, Ohnuma T, Numata T, Suzuki A, Usui T, Fukamizo T J Biol Chem. 2013 Mar 1;288(9):6072-82. doi: 10.1074/jbc.M112.439281. Epub 2013, Jan 9. PMID:23303182[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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