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.


1lzd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1lzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lzd, resolution 1.8&Aring;" /> '''DISSECTION OF PROTEIN...)
Current revision (08:29, 10 April 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1lzd.jpg|left|200px]]<br /><applet load="1lzd" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1lzd, resolution 1.8&Aring;" />
 
-
'''DISSECTION OF PROTEIN-CARBOHYDRATE INTERACTIONS IN MUTANT HEN EGG-WHITE LYSOZYME COMPLEXES AND THEIR HYDROLYTIC ACTIVITY'''<br />
 
-
==Overview==
+
==DISSECTION OF PROTEIN-CARBOHYDRATE INTERACTIONS IN MUTANT HEN EGG-WHITE LYSOZYME COMPLEXES AND THEIR HYDROLYTIC ACTIVITY==
-
Trp62 in the binding subsite B of hen egg-white lysozyme shows general, features often observed in protein-carbohydrate interactions including a, stacking interaction and a hydrogen bonding network with water molecules., A previous report by our group showed that the perturbation of these, interactions by substitution of Trp62 with tyrosine or phenylalanine, affects the substrate binding modes and also enhances the hydrolytic, activity. In order to elucidate the relationship between structural and, functional changes of these protein-carbohydrate interactions, the, Trp62Tyr and Trp62Phe mutants complexed with the substrate analogue, (GlcNAc)3, were analyzed at 1.8 A resolution by X-ray crystallography. The, overall structures of the mutant enzymes are indistinguishable from that, of the wild type enzyme. Although the wild-type enzyme binds (GlcNAc)3 in, only one binding mode (A-B-C), the Trp62Tyr mutant binds (GlcNAc)3 in two, binding modes (A-B-C, B-C-D) and the Trp62Phe mutant has an even weaker, binding mode. The aromatic rings of Tyr62 and Phe62 maintain their, interactions with the carbohydrate molecules, but make fewer stacking, interactions with the GlcNAc in the B site than the wild-type enzyme does., The hydroxyl group of Tyr62 interacts weakly with a water molecule which, mediates hydrogen bonding in the GlcNAc residues in the B and C sites. The, C-6 hydroxyl group of the GlcNAc residue in the C site rotates around the, C-5-C-6 bond to complete the hydrogen bond network in the Trp62Tyr, mutant-(GlcNAc)3 complex. On the other hand, this hydrogen bonding network, does not form in the Trp62Phe mutant-(GlcNAc)3. In addition to these, structural studies, the kinetic parameters of the hydrolysis of, 4-methylumbelliferyl N-acetyl-chitotriose, ((GlcNAc)3-MeU), have been, determined in order to further characterize the enzymatic properties of, these mutant lysozymes. This demonstrates that the modulation of the, hydrogen bonding network, including the flexible part of the carbohydrate, and water molecules and/or the slight reduction of stacking interaction in, the B site, alters the binding mode toward the carbohydrate and induces an, enhancement of the hydrolytic activity.
+
<StructureSection load='1lzd' size='340' side='right'caption='[[1lzd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1lzd]] 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=1LZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LZD 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]] 1.8&#8491;</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=1lzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lzd OCA], [https://pdbe.org/1lzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lzd RCSB], [https://www.ebi.ac.uk/pdbsum/1lzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lzd 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/1lzd_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=1lzd ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1LZD 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=1LZD OCA].
+
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity., Maenaka K, Matsushima M, Song H, Sunada F, Watanabe K, Kumagai I, J Mol Biol. 1995 Mar 24;247(2):281-93. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7707375 7707375]
+
__TOC__
 +
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
-
[[Category: Lysozyme]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Kumagai I]]
-
[[Category: Kumagai, I.]]
+
[[Category: Maenaka K]]
-
[[Category: Maenaka, K.]]
+
[[Category: Matsushima M]]
-
[[Category: Matsushima, M.]]
+
[[Category: Song H]]
-
[[Category: Song, H.]]
+
[[Category: Watanabe K]]
-
[[Category: Watanabe, K.]]
+
-
[[Category: hydrolase (o-glycosyl)]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:00:33 2007''
+

Current revision

DISSECTION OF PROTEIN-CARBOHYDRATE INTERACTIONS IN MUTANT HEN EGG-WHITE LYSOZYME COMPLEXES AND THEIR HYDROLYTIC ACTIVITY

PDB ID 1lzd

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/1lzd"
Personal tools