6apm: Difference between revisions
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New page: '''Unreleased structure''' The entry 6apm is ON HOLD Authors: Lyubimov, A.Y., Mathews, I.I., Uervivojnangkoorn, M., Soltis, S.M., Cohen, A.E. Description: Hen egg-white lysozyme (WT), ... |
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==Hen egg-white lysozyme (WT), solved with serial millisecond crystallography using synchrotron radiation== | |||
<StructureSection load='6apm' size='340' side='right'caption='[[6apm]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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='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> | |||
</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 == | |||
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<ref>PMID:28832129</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Cohen | <div class="pdbe-citations 6apm" style="background-color:#fffaf0;"></div> | ||
[[Category: Lyubimov | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Cohen AE]] | |||
[[Category: Lyubimov AY]] | |||
[[Category: Mathews II]] | |||
[[Category: Soltis SM]] | |||
[[Category: Uervivojnangkoorn M]] | |||
Latest revision as of 14:22, 4 October 2023
Hen egg-white lysozyme (WT), solved with serial millisecond crystallography using synchrotron radiation
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