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4r6c

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Revision as of 18:46, 1 February 2017

X-ray diffraction in temporally and spatially resolved biomolecular science: the X-ray crystal structure of hen egg white lysozyme cocrystallized with Ta6Br12 and then a crystal soaked in K2PtBr6

Structural highlights

4r6c is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	4owh
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Time-resolved Laue protein crystallography at the European Synchrotron Radiation Facility (ESRF) opened up the field of sub-nanosecond protein crystal structure analyses. There are a limited number of such time-resolved studies in the literature. Why is this? The X-ray laser now gives us femtosecond (fs) duration pulses, typically 10 fs up to approximately 50 fs. Their use is attractive for the fastest time-resolved protein crystallography studies. It has been proposed that single molecules could even be studied with the advantage of being able to measure X-ray diffraction from a 'crystal lattice free' single molecule, with or without temporal resolved structural changes. This is altogether very challenging R&D. So as to assist this effort we have undertaken studies of metal clusters that bind to proteins, both 'fresh' and after repeated X-ray irradiation to assess their X-ray-photo-dynamics, namely Ta6Br12, K2PtI6 and K2PtBr6 bound to a test protein, hen egg white lysozyme. These metal complexes have the major advantage of being very recognisable shapes (pseudo spherical or octahedral) and thereby offer a start to (probably very difficult) single molecule electron density map interpretations, both static and dynamic. A further approach is to investigate the X-ray laser beam diffraction strength of a well scattering nano-cluster; an example from nature being the iron containing ferritin. Electron crystallography and single particle electron microscopy imaging offers alternatives to X-ray structural studies; our structural studies of crustacyanin, a 320 kDa protein carotenoid complex, can be extended either by electron based techniques or with the X-ray laser representing a fascinating range of options. General outlook remarks concerning X-ray, electron and neutron macromolecular crystallography as well as 'NMR crystallography' conclude the article.

X-ray diffraction in temporally and spatially resolved biomolecular science.,Helliwell JR, Brink A, Kaenket S, Starkey VL, Tanley SW Faraday Discuss. 2015 Jan 21. PMID:25605312^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Helliwell JR, Brink A, Kaenket S, Starkey VL, Tanley SW. X-ray diffraction in temporally and spatially resolved biomolecular science. Faraday Discuss. 2015 Jan 21. PMID:25605312 doi:http://dx.doi.org/10.1039/c4fd00166d

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4r6c"

Categories: Gallus gallus | Lysozyme | Helliwell, J R | Hydrolase | Ta6br12 and ptbr6

@@ Line 1: / Line 1: @@
 ==X-ray diffraction in temporally and spatially resolved biomolecular science: the X-ray crystal structure of hen egg white lysozyme cocrystallized with Ta6Br12 and then a crystal soaked in K2PtBr6==
 <StructureSection load='4r6c' size='340' side='right' caption='[[4r6c]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4owh|4owh]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r6c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r6c RCSB], [http://www.ebi.ac.uk/pdbsum/4r6c PDBsum]</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=4r6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r6c OCA], [http://pdbe.org/4r6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r6c RCSB], [http://www.ebi.ac.uk/pdbsum/4r6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r6c ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4r6c" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4r6c

From Proteopedia

Revision as of 18:46, 1 February 2017

X-ray diffraction in temporally and spatially resolved biomolecular science: the X-ray crystal structure of hen egg white lysozyme cocrystallized with Ta6Br12 and then a crystal soaked in K2PtBr6

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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