3gxr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3gxr" [edit=sysop:move=sysop])
Current revision (15:45, 1 November 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3gxr.png|left|200px]]
 
-
{{STRUCTURE_3gxr| PDB=3gxr | SCENE= }}
+
==The crystal structure of g-type lysozyme from Atlantic cod (Gadus morhua L.) in complex with NAG oligomers sheds new light on substrate binding and the catalytic mechanism. Structure with NAG to 1.7==
 +
<StructureSection load='3gxr' size='340' side='right'caption='[[3gxr]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3gxr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gadus_morhua Gadus morhua]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GXR 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]] 1.7&#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>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</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=3gxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gxr OCA], [https://pdbe.org/3gxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gxr RCSB], [https://www.ebi.ac.uk/pdbsum/3gxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gxr ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/B9TU22_GADMO B9TU22_GADMO]
 +
== 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/gx/3gxr_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=3gxr ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Crystal structures of Atlantic cod lysozyme have been solved with and without ligand bound in the active site to 1.7 and 1.9 A resolution, respectively. The structures reveal the presence of NAG in the substrate binding sites at both sides of the catalytic Glu73, hence allowing the first crystallographic description of the goose-type (g-type) lysozyme E-G binding sites. In addition, two aspartic acid residues suggested to participate in catalysis (Asp101 and Asp90) were mutated to alanine. Muramidase activity data for two single mutants and one double mutant demonstrates that both residues are involved in catalysis, but Asp101 is the more critical of the two. The structures and activity data suggest that a water molecule is the nucleophile completing the catalytic reaction, and the roles of the aspartic acids are to ensure proper positioning of the catalytic water.
-
===The crystal structure of g-type lysozyme from Atlantic cod (Gadus morhua L.) in complex with NAG oligomers sheds new light on substrate binding and the catalytic mechanism. Structure with NAG to 1.7===
+
Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism.,Helland R, Larsen RL, Finstad S, Kyomuhendo P, Larsen AN Cell Mol Life Sci. 2009 Aug;66(15):2585-98. Epub 2009 Jun 20. PMID:19543850<ref>PMID:19543850</ref>
-
{{ABSTRACT_PUBMED_19543850}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 3gxr" style="background-color:#fffaf0;"></div>
-
[[3gxr]] is a 4 chain structure of [[Hen Egg-White (HEW) Lysozyme]] with sequence from [http://en.wikipedia.org/wiki/Gadus_morhua Gadus morhua]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GXR 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:019543850</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Gadus morhua]]
[[Category: Gadus morhua]]
-
[[Category: Lysozyme]]
+
[[Category: Large Structures]]
-
[[Category: Finstad, S.]]
+
[[Category: Finstad S]]
-
[[Category: Helland, R.]]
+
[[Category: Helland R]]
-
[[Category: Kyomuhendo, P.]]
+
[[Category: Kyomuhendo P]]
-
[[Category: Larsen, A N.]]
+
[[Category: Larsen AN]]
-
[[Category: Larsen, R L.]]
+
[[Category: Larsen RL]]
-
[[Category: Active site residue]]
+
-
[[Category: Atlantic cod]]
+
-
[[Category: Fish lysozyme]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Immune system]]
+
-
[[Category: Muramidase activity]]
+
-
[[Category: Substrate binding site]]
+
-
[[Category: Surface potential]]
+

Current revision

The crystal structure of g-type lysozyme from Atlantic cod (Gadus morhua L.) in complex with NAG oligomers sheds new light on substrate binding and the catalytic mechanism. Structure with NAG to 1.7

PDB ID 3gxr

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/3gxr"
Personal tools