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1ehd

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CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ ISOLECTIN VI

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Retrieved from "http://52.214.119.220/wiki/index.php/1ehd"

Categories: Large Structures | Urtica dioica | Harata K | Muraki M

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-[[Image:1ehd.gif|left|200px]]<br /><applet load="1ehd" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ehd, resolution 1.5&Aring;" />
-'''CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ ISOLECTIN VI'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ ISOLECTIN VI==
-Urtica dioica agglutinin is a small plant lectin that binds chitin. We, purified the isolectin VI (UDA-VI) and crystal structures of the isolectin, and its complex with tri-N-acetylchitotriose (NAG3) were determined by, X-ray analysis. The UDA-VI consists of two domains analogous to hevein and, the backbone folding of each domain is maintained by four disulfide, bridges. The sequence similarity of the two domains is not high (42 %) but, their backbone structures are well superimposed except some loop regions., The chitin binding sites are located on the molecular surface at both ends, of the dumbbell-shape molecule. The crystal of the NAG3 complex contains, two independent molecules forming a protein-sugar 2:2 complex. One NAG3, molecule is sandwiched between two independent UDA-VI molecules and the, other sugar molecule is also sandwiched by one UDA-VI molecule and, symmetry-related another one. The sugar binding site of N-terminal domain, consists of three subsites accommodating NAG3 while two NAG residues are, bound to the C-terminal domain. In each sugar-binding site, three aromatic, amino acid residues and one serine residue participate to the NAG3, binding. The sugar rings bound to two subsites are stacked to the, side-chain groups of tryptophan or histidine and a tyrosine residue is in, face-to-face contact with an acetylamino group, to which the hydroxyl, group of a serine residue is hydrogen-bonded. The third subsite of the, N-terminal domain binds a NAG moiety with hydrogen bonds. The results, suggest that the triad of aromatic amino acid residues is intrinsic in, sugar binding of hevein-like domains.
+<StructureSection load='1ehd' size='340' side='right'caption='[[1ehd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ehd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Urtica_dioica Urtica dioica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EHD 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]] 1.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=1ehd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehd OCA], [https://pdbe.org/1ehd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ehd RCSB], [https://www.ebi.ac.uk/pdbsum/1ehd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ehd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9S7B3_URTDI Q9S7B3_URTDI]
+== 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/eh/1ehd_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=1ehd ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-EHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Urtica_dioica Urtica dioica]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EHD OCA].
+*[[Agglutinin 3D structures|Agglutinin 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structures of Urtica dioica agglutinin and its complex with tri-N-acetylchitotriose., Harata K, Muraki M, J Mol Biol. 2000 Mar 31;297(3):673-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10731420 10731420]
+[[Category: Large Structures]]
-[[Category: Single protein]]
 [[Category: Urtica dioica]]
-[[Category: Harata, K.]]
+[[Category: Harata K]]
-[[Category: Muraki, M.]]
+[[Category: Muraki M]]
-[[Category: two homologous hevein-like domains]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:15:47 2007''

1ehd

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CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ ISOLECTIN VI

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Function

Evolutionary Conservation

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