|
|
| (2 intermediate revisions not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4b4j' size='340' side='right'caption='[[4b4j]], [[Resolution|resolution]] 1.25Å' scene=''> | | <StructureSection load='4b4j' size='340' side='right'caption='[[4b4j]], [[Resolution|resolution]] 1.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b4j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B4J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B4J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b4j]] 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=4B4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B4J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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]] 1.25Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b49|4b49]], [[4b4e|4b4e]], [[4b4i|4b4i]]</td></tr> | + | <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=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=4b4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4j OCA], [https://pdbe.org/4b4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b4j RCSB], [https://www.ebi.ac.uk/pdbsum/4b4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4j ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b4j OCA], [http://pdbe.org/4b4j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b4j RCSB], [http://www.ebi.ac.uk/pdbsum/4b4j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b4j ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 29: |
Line 28: |
| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Asherie N]] |
| - | [[Category: Asherie, N]] | + | [[Category: Axelbaum A]] |
| - | [[Category: Axelbaum, A]] | + | [[Category: Berger J]] |
| - | [[Category: Berger, J]] | + | [[Category: Jakoncic J]] |
| - | [[Category: Jakoncic, J]] | + | [[Category: Stauber M]] |
| - | [[Category: Stauber, M]] | + | |
| - | [[Category: Chirality]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
Chiral control of crystallization has ample precedent in the small-molecule world, but relatively little is known about the role of chirality in protein crystallization. In this study, lysozyme was crystallized in the presence of the chiral additive 2-methyl-2,4-pentanediol (MPD) separately using the R and S enantiomers as well as with a racemic RS mixture. Crystals grown with (R)-MPD had the most order and produced the highest resolution protein structures. This result is consistent with the observation that in the crystals grown with (R)-MPD and (RS)-MPD the crystal contacts are made by (R)-MPD, demonstrating that there is preferential interaction between lysozyme and this enantiomer. These findings suggest that chiral interactions are important in protein crystallization.
Crystallization of lysozyme with (R)-, (S)- and (RS)-2-methyl-2,4-pentanediol.,Stauber M, Jakoncic J, Berger J, Karp JM, Axelbaum A, Sastow D, Buldyrev SV, Hrnjez BJ, Asherie N Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):427-41. doi:, 10.1107/S1399004714025061. Epub 2015 Feb 26. PMID:25760593[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
- ↑ Stauber M, Jakoncic J, Berger J, Karp JM, Axelbaum A, Sastow D, Buldyrev SV, Hrnjez BJ, Asherie N. Crystallization of lysozyme with (R)-, (S)- and (RS)-2-methyl-2,4-pentanediol. Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):427-41. doi:, 10.1107/S1399004714025061. Epub 2015 Feb 26. PMID:25760593 doi:http://dx.doi.org/10.1107/S1399004714025061
|
