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| | <StructureSection load='6apm' size='340' side='right'caption='[[6apm]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='6apm' size='340' side='right'caption='[[6apm]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6apm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6APM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6APM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6apm]] 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=6APM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6APM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 2.05Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6apk|6apk]], [[6apg|6apg]], [[6apf|6apf]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=6apm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6apm OCA], [https://pdbe.org/6apm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6apm RCSB], [https://www.ebi.ac.uk/pdbsum/6apm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6apm ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6apm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6apm OCA], [http://pdbe.org/6apm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6apm RCSB], [http://www.ebi.ac.uk/pdbsum/6apm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6apm 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 == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Cohen AE]] |
| - | [[Category: Cohen, A E]] | + | [[Category: Lyubimov AY]] |
| - | [[Category: Lyubimov, A Y]] | + | [[Category: Mathews II]] |
| - | [[Category: Mathews, I I]] | + | [[Category: Soltis SM]] |
| - | [[Category: Soltis, S M]] | + | [[Category: Uervivojnangkoorn M]] |
| - | [[Category: Uervivojnangkoorn, M]] | + | |
| - | [[Category: Hewl]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Serial millisecond crystallography]]
| + | |
| - | [[Category: Xfel crystal structure]]
| + | |
| 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
The crystal structure of the trans-acyltransferase (AT) from the disorazole polyketide synthase (PKS) was determined at room temperature to a resolution of 2.5 A using a new method for the direct delivery of the sample into an X-ray free-electron laser. A novel sample extractor efficiently delivered limited quantities of microcrystals directly from the native crystallization solution into the X-ray beam at room temperature. The AT structure revealed important catalytic features of this core PKS enzyme, including the occurrence of conformational changes around the active site. The implications of these conformational changes for polyketide synthase reaction dynamics are discussed.
The Conformational Flexibility of the Acyltransferase from the Disorazole Polyketide Synthase Is Revealed by an X-ray Free-Electron Laser Using a Room-Temperature Sample Delivery Method for Serial Crystallography.,Mathews II, Allison K, Robbins T, Lyubimov AY, Uervirojnangkoorn M, Brunger AT, Khosla C, DeMirci H, McPhillips SE, Hollenbeck M, Soltis M, Cohen AE Biochemistry. 2017 Sep 12;56(36):4751-4756. doi: 10.1021/acs.biochem.7b00711., Epub 2017 Aug 31. PMID:28832129[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
- ↑ Mathews II, Allison K, Robbins T, Lyubimov AY, Uervirojnangkoorn M, Brunger AT, Khosla C, DeMirci H, McPhillips SE, Hollenbeck M, Soltis M, Cohen AE. The Conformational Flexibility of the Acyltransferase from the Disorazole Polyketide Synthase Is Revealed by an X-ray Free-Electron Laser Using a Room-Temperature Sample Delivery Method for Serial Crystallography. Biochemistry. 2017 Sep 12;56(36):4751-4756. doi: 10.1021/acs.biochem.7b00711., Epub 2017 Aug 31. PMID:28832129 doi:http://dx.doi.org/10.1021/acs.biochem.7b00711
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