9lyz

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(New page: 200px<br /><applet load="9lyz" size="350" color="white" frame="true" align="right" spinBox="true" caption="9lyz, resolution 2.5&Aring;" /> '''X-RAY CRYSTALLOGRAPHY...)
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[[Image:9lyz.gif|left|200px]]<br /><applet load="9lyz" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="9lyz, resolution 2.5&Aring;" />
 
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'''X-RAY CRYSTALLOGRAPHY OF THE BINDING OF THE BACTERIAL CELL WALL TRISACCHARIDE NAM-NAG-NAM TO LYSOZYME'''<br />
 
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==Overview==
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==X-RAY CRYSTALLOGRAPHY OF THE BINDING OF THE BACTERIAL CELL WALL TRISACCHARIDE NAM-NAG-NAM TO LYSOZYME==
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Hen egg white lysozyme was the first enzyme whose structure was determined, by X-ray crystallography. The proposed mechanism based on this structure, involves the distortion of the saccharide residue, (2-acetamido-2-deoxy-D-muramic acid, NAM) in the natural substrate (an, alternating beta (1 leads to 4) linked oligomer of, 2-acetamido-2-deoxy-D-glucose (NAG) and NAM residues) bound to site D in, the binding cleft. The importance of substrate distortion has prompted, numerous enzymatic, chemical, theoretical, and physical studies, but there, is little direct crystallographic evidence on the conformation of a NAM, residue bound at site D. We now present the X-ray structure of the, non-hydrolysed trisaccharide NAM-NAG-NAM bound in subsites B, C, D. Our, interpretation of the 2.5-A resolution difference map does not involve, distortion of this residue in site D. Comparison with the structure of the, delta-lactone derived from tetra N-acetylchitotetraose (NAG)3NAL) bound to, lysozyme suggests we may be looking at a Michaelis complex.
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<StructureSection load='9lyz' size='340' side='right'caption='[[9lyz]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9lyz]] 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=9LYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LYZ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMU:BETA-N-ACETYLMURAMIC+ACID'>AMU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9lyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lyz OCA], [https://pdbe.org/9lyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lyz RCSB], [https://www.ebi.ac.uk/pdbsum/9lyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lyz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hen egg white lysozyme was the first enzyme whose structure was determined by X-ray crystallography. The proposed mechanism based on this structure involves the distortion of the saccharide residue (2-acetamido-2-deoxy-D-muramic acid, NAM) in the natural substrate (an alternating beta (1 leads to 4) linked oligomer of 2-acetamido-2-deoxy-D-glucose (NAG) and NAM residues) bound to site D in the binding cleft. The importance of substrate distortion has prompted numerous enzymatic, chemical, theoretical, and physical studies, but there is little direct crystallographic evidence on the conformation of a NAM residue bound at site D. We now present the X-ray structure of the non-hydrolysed trisaccharide NAM-NAG-NAM bound in subsites B, C, D. Our interpretation of the 2.5-A resolution difference map does not involve distortion of this residue in site D. Comparison with the structure of the delta-lactone derived from tetra N-acetylchitotetraose (NAG)3NAL) bound to lysozyme suggests we may be looking at a Michaelis complex.
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==About this Structure==
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X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme.,Kelly JA, Sielecki AR, Sykes BD, James MN, Phillips DC Nature. 1979 Dec 20-27;282(5741):875-8. PMID:514367<ref>PMID:514367</ref>
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9LYZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LYZ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme., Kelly JA, Sielecki AR, Sykes BD, James MN, Phillips DC, Nature. 1979 Dec 20-27;282(5741):875-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=514367 514367]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 9lyz" style="background-color:#fffaf0;"></div>
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[[Category: James, M.N.G.]]
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[[Category: Kelly, J.A.]]
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[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:54:13 2008''
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: James MNG]]
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[[Category: Kelly JA]]

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X-RAY CRYSTALLOGRAPHY OF THE BINDING OF THE BACTERIAL CELL WALL TRISACCHARIDE NAM-NAG-NAM TO LYSOZYME

PDB ID 9lyz

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