1lz8: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "1lz8" [edit=sysop:move=sysop]
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1lz8.png|left|200px]]


{{STRUCTURE_1lz8| PDB=1lz8 | SCENE= }}
==LYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINES==
<StructureSection load='1lz8' size='340' side='right'caption='[[1lz8]], [[Resolution|resolution]] 1.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lz8]] 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=1LZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LZ8 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]] 1.53&#8491;</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=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=1lz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lz8 OCA], [https://pdbe.org/1lz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lz8 RCSB], [https://www.ebi.ac.uk/pdbsum/1lz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lz8 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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lz/1lz8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lz8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A general method for solving the phase problem from native crystals of macromolecules has long eluded structural biology. For well diffracting crystals this goal can now be achieved, as is shown here, thanks to modern data collection techniques and new statistical phasing algorithms. Using solely a native crystal of tetragonal hen egg-white lysozyme, a protein of 14 kDa molecular mass, it was possible to detect the positions of the ten sulfur and seven chlorine atoms from their anomalous signal, and proceed from there to obtain an electron-density map of very high quality.


===LYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINES===
Can anomalous signal of sulfur become a tool for solving protein crystal structures?,Dauter Z, Dauter M, de La Fortelle E, Bricogne G, Sheldrick GM J Mol Biol. 1999 May 28;289(1):83-92. PMID:10339407<ref>PMID:10339407</ref>


{{ABSTRACT_PUBMED_10339407}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1lz8" style="background-color:#fffaf0;"></div>
[[1lz8]] is a 1 chain structure of [[Hen Egg-White (HEW) Lysozyme]] 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=1LZ8 OCA].


==See Also==
==See Also==
*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:010339407</ref><ref group="xtra">PMID:011679726</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Bricogne, G.]]
[[Category: Bricogne G]]
[[Category: Dauter, M.]]
[[Category: Dauter M]]
[[Category: Dauter, Z.]]
[[Category: Dauter Z]]
[[Category: Fortelle, E De La.]]
[[Category: De La Fortelle E]]
[[Category: Sheldrick, G M.]]
[[Category: Sheldrick GM]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: O-glycosyl]]

Latest revision as of 03:13, 21 November 2024

LYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINESLYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINES

Structural highlights

1lz8 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.
Method:X-ray diffraction, Resolution 1.53Å
Ligands:,
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

A general method for solving the phase problem from native crystals of macromolecules has long eluded structural biology. For well diffracting crystals this goal can now be achieved, as is shown here, thanks to modern data collection techniques and new statistical phasing algorithms. Using solely a native crystal of tetragonal hen egg-white lysozyme, a protein of 14 kDa molecular mass, it was possible to detect the positions of the ten sulfur and seven chlorine atoms from their anomalous signal, and proceed from there to obtain an electron-density map of very high quality.

Can anomalous signal of sulfur become a tool for solving protein crystal structures?,Dauter Z, Dauter M, de La Fortelle E, Bricogne G, Sheldrick GM J Mol Biol. 1999 May 28;289(1):83-92. PMID:10339407[2]

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

See Also

References

  1. 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
  2. Dauter Z, Dauter M, de La Fortelle E, Bricogne G, Sheldrick GM. Can anomalous signal of sulfur become a tool for solving protein crystal structures? J Mol Biol. 1999 May 28;289(1):83-92. PMID:10339407 doi:10.1006/jmbi.1999.2743

1lz8, resolution 1.53Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA