1dq6: Difference between revisions

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[[Image:1dq6.jpg|left|200px]]


{{Structure
==Manganese;Manganese concanavalin A at pH 7.0==
|PDB= 1dq6 |SIZE=350|CAPTION= <scene name='initialview01'>1dq6</scene>, resolution 1.9&Aring;
<StructureSection load='1dq6' size='340' side='right'caption='[[1dq6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene>
<table><tr><td colspan='2'>[[1dq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQ6 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1dq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dq6 OCA], [https://pdbe.org/1dq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1dq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dq6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CONA_CANEN CONA_CANEN] D-mannose specific lectin.
== 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/dq/1dq6_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=1dq6 ConSurf].
<div style="clear:both"></div>


'''Manganese;Manganese concanavalin A at pH 7.0'''
==See Also==
 
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The reversible binding of manganese and calcium to concanavalin A determines the carbohydrate binding of the lectin by inducing large conformational changes. These changes are governed by the isomerization of a non-proline peptide bond, Ala-207-Asp-208, positioned in a beta-strand in between the calcium binding site S2 and the carbohydrate specificity-determining loop. The replacement of calcium by manganese allowed us to investigate the structures of the carbohydrate binding, locked state and the inactive, unlocked state of concanavalin A, both with and without metal ions bound. Crystals of unlocked metal-free concanavalin A convert to the locked form with the binding of two Mn(2+) ions. Removal of these ions from the crystals traps metal-free concanavalin A in its locked state, a minority species in solution. The ligation of a metal ion in S2 to unlocked concanavalin A causes bending of the beta-strand foregoing the S2 ligand residues Asp-10 and Tyr-12. This bending disrupts conventional beta-sheet hydrogen bonding and forces the Thr-11 side chain against the Ala-207-Asp-208 peptide bond. The steric strain exerted by Thr-11 is presumed to drive the trans-to-cis isomerization. Upon isomerization, Asp-208 flips into its carbohydrate binding position, and the conformation of the carbohydrate specificity determining loop changes dramatically.
 
==About this Structure==
1DQ6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQ6 OCA].
 
==Reference==
The structural features of concanavalin A governing non-proline peptide isomerization., Bouckaert J, Dewallef Y, Poortmans F, Wyns L, Loris R, J Biol Chem. 2000 Jun 30;275(26):19778-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10748006 10748006]
[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bouckaert, J.]]
[[Category: Bouckaert J]]
[[Category: Dewallef, Y.]]
[[Category: Dewallef Y]]
[[Category: Loris, R.]]
[[Category: Loris R]]
[[Category: Poortmans, F.]]
[[Category: Poortmans F]]
[[Category: Wyns, L.]]
[[Category: Wyns L]]
[[Category: MN]]
[[Category: binuclear]]
[[Category: concanavalin some]]
[[Category: lectin]]
[[Category: manganese]]
[[Category: metal binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:42:30 2008''

Latest revision as of 09:57, 7 February 2024

Manganese;Manganese concanavalin A at pH 7.0Manganese;Manganese concanavalin A at pH 7.0

Structural highlights

1dq6 is a 1 chain structure with sequence from Canavalia ensiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CONA_CANEN D-mannose specific lectin.

Evolutionary Conservation

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

See Also

1dq6, resolution 1.90Å

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OCA
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