1cjp: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1cjp.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1cjp", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1cjp|  PDB=1cjp  |  SCENE=  }}
'''CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE'''


==CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE==
<StructureSection load='1cjp' size='340' side='right'caption='[[1cjp]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cjp]] is a 4 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=1CJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJP 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]] 2.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MUG:4-METHYLUMBELLIFERYL-ALPHA-D-GLUCOSE'>MUG</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=1cjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjp OCA], [https://pdbe.org/1cjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjp RCSB], [https://www.ebi.ac.uk/pdbsum/1cjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjp 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/cj/1cjp_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=1cjp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Concanavalin A (Con A) is the best known plant lectin, with important biological properties arising from its specific saccharide-binding ability. Its exact biological role still remains unknown. The complex of Con A with 4'-methylumbelliferyl-alpha-D-glucopyranoside (alpha-MUG) has been crystallized in space group P2(1) with cell dimensions a = 81.62 A, b = 128.71 A, c = 82.23 A, and beta = 118.47 degrees. X-ray diffraction intensities to 2.78 A have been collected. The structure of the complex was solved by molecular replacement and refined by simulated annealing methods to a crystallographic R-factor value of 0.182 and a free-R-factor value of 0.216. The asymmetric unit contains four subunits arranged as a tetramer, with approximate 222 symmetry. A saccharide molecule is bound in the sugar-binding site at the surface of each subunit, with the nonsugar (aglycon) part adopting a different orientation in each subunit. The aglycon orientation, although probably determined by packing of tetramers in the crystal lattice, helps to characterize the orientation of the saccharide in the sugar-binding pocket. The structure is the best determined alpha-D-glucoside:Con A complex to date and the hydrogen bonding network in the saccharide-binding site can be described with some confidence and compared with that of the alpha-D-mannosides.


==Overview==
The crystal structure of the complex of concanavalin A with 4'-methylumbelliferyl-alpha-D-glucopyranoside.,Hamodrakas SJ, Kanellopoulos PN, Pavlou K, Tucker PA J Struct Biol. 1997 Feb;118(1):23-30. PMID:9087912<ref>PMID:9087912</ref>
Concanavalin A (Con A) is the best known plant lectin, with important biological properties arising from its specific saccharide-binding ability. Its exact biological role still remains unknown. The complex of Con A with 4'-methylumbelliferyl-alpha-D-glucopyranoside (alpha-MUG) has been crystallized in space group P2(1) with cell dimensions a = 81.62 A, b = 128.71 A, c = 82.23 A, and beta = 118.47 degrees. X-ray diffraction intensities to 2.78 A have been collected. The structure of the complex was solved by molecular replacement and refined by simulated annealing methods to a crystallographic R-factor value of 0.182 and a free-R-factor value of 0.216. The asymmetric unit contains four subunits arranged as a tetramer, with approximate 222 symmetry. A saccharide molecule is bound in the sugar-binding site at the surface of each subunit, with the nonsugar (aglycon) part adopting a different orientation in each subunit. The aglycon orientation, although probably determined by packing of tetramers in the crystal lattice, helps to characterize the orientation of the saccharide in the sugar-binding pocket. The structure is the best determined alpha-D-glucoside:Con A complex to date and the hydrogen bonding network in the saccharide-binding site can be described with some confidence and compared with that of the alpha-D-mannosides.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1CJP 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=1CJP OCA].
</div>
<div class="pdbe-citations 1cjp" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The crystal structure of the complex of concanavalin A with 4'-methylumbelliferyl-alpha-D-glucopyranoside., Hamodrakas SJ, Kanellopoulos PN, Pavlou K, Tucker PA, J Struct Biol. 1997 Feb;118(1):23-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9087912 9087912]
*[[Concanavalin 3D structures|Concanavalin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hamodrakas, S J.]]
[[Category: Hamodrakas SJ]]
[[Category: Kanellopoulos, P N.]]
[[Category: Kanellopoulos PN]]
[[Category: Tucker, P A.]]
[[Category: Tucker PA]]
[[Category: Legume lectin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:48:22 2008''
Retrieved from "https://proteopedia.org/1cjp"