This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1sf4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1sf4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sf4, resolution 2.98&Aring;" /> '''BINDING OF N,N'-DIAC...)
Current revision (08:31, 1 May 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1sf4.jpg|left|200px]]<br /><applet load="1sf4" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1sf4, resolution 2.98&Aring;" />
 
-
'''BINDING OF N,N'-DIACETYLCHITOBIOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY'''<br />
 
-
==Overview==
+
==BINDING OF N,N'-DIACETYLCHITOBIOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY==
-
The binding of N-acetylglucosamine oligosaccharides (NAGn, n = 2-6) to hen, egg-white lysozyme (HEWL; EC 3.2.1.17) was investigated by X-ray powder, diffraction at room temperature. Each NAGn examined was found to bind to, lysozyme in rapid-precipitation preparations in 1.0 M NaCl pH 6.0 buffer., The location of each NAGn was easily found from difference Fourier maps, generated from structure factors extracted during preliminary Rietveld, refinements. Full NAGn-protein structures were subjected to combined, Rietveld and stereochemical restraint refinements (Rwp = 2.28-2.59%; Rp =, 1.81-2.04%; RF2 = 3.91-5.80%) and revealed binding modes for NAGn that, depended on the length of the NAG oligosaccharide. The NAG2 ligand was, found in the BC sites in the cleft of HEWL, NAG3 was found to bind in both, the ABC and BCD sites in the ratio 35:65 and NAG4 and NAG5 bound to the, ABCD and ABCDE sites, respectively, while NAG6 only bound to sites ABCDE, leaving the F site empty with the remaining saccharide ring located in a, solvent region adjacent to the A site. All protein powder diffraction, patterns in this study consisted of extremely sharp Bragg peaks consistent, with approximately 1 microm crystallites that were devoid of, line-broadening defects. Details of the stereochemical restraints used in, these refinements and their impact on structural validation are also, discussed.
+
<StructureSection load='1sf4' size='340' side='right'caption='[[1sf4]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1sf4]] 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=1SF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SF4 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray powder diffraction, [[Resolution|Resolution]] 2.98&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1sf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sf4 OCA], [https://pdbe.org/1sf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sf4 RCSB], [https://www.ebi.ac.uk/pdbsum/1sf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sf4 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/sf/1sf4_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1sf4 ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1SF4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SF4 OCA].
+
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
Binding of N-acetylglucosamine oligosaccharides to hen egg-white lysozyme: a powder diffraction study., Von Dreele RB, Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):22-32. Epub 2004, Dec 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15608372 15608372]
+
__TOC__
 +
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
-
[[Category: Lysozyme]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Von Dreele RB]]
-
[[Category: Dreele, R.B.Von.]]
+
-
[[Category: powder diffraction; rietveld refinement; lysozyme]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:20:09 2007''
+

Current revision

BINDING OF N,N'-DIACETYLCHITOBIOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY

PDB ID 1sf4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sf4"
Personal tools