1fay: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1fay" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fay, resolution 3.30Å" /> '''WINGED BEAN ACIDIC L...
 
OCA (talk | contribs)
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1fay.gif|left|200px]]<br /><applet load="1fay" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fay, resolution 3.30&Aring;" />
'''WINGED BEAN ACIDIC LECTIN COMPLEXED WITH METHYL-ALPHA-D-GALACTOSE (MONOCLINIC FORM)'''<br />


==Overview==
==WINGED BEAN ACIDIC LECTIN COMPLEXED WITH METHYL-ALPHA-D-GALACTOSE (MONOCLINIC FORM)==
Structures of two crystal forms of the dimeric acidic winged bean, agglutinin (WBAII) complexed with methyl-alpha-D-galactose have been, determined at 3.0 A and 3.3 A resolution. The subunit structure and, dimerisation of the lectin are similar to those of the basic lectin from, winged bean (WBAI) and the lectin from Erythrina corallodendron (EcorL)., The conformation of a loop and its orientation with respect to the rest of, the molecule in WBAII are, however, different from those in all the other, legume lectins of known structure. This difference appears to have been, caused by the formation of two strategically placed salt bridges in the, former. Modelling based on the crystal structures provides a rationale for, the specificity of the lectin, which is very different from that of WBAI, for the H-antigenic determinant responsible for O blood group reactivity., It also leads to a qualitative explanation for the thermodynamic data on, sugar-binding to the lectin, with special emphasis on the role of a, tyrosyl residue in the variable loop in the sugar-binding region in, generating the carbohydrate specificity of WBAII.
<StructureSection load='1fay' size='340' side='right'caption='[[1fay]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fay]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAY 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]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMG:ALPHA-METHYL-D-GALACTOSIDE'>AMG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1fay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fay OCA], [https://pdbe.org/1fay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fay RCSB], [https://www.ebi.ac.uk/pdbsum/1fay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fay ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9SM56_PSOTE Q9SM56_PSOTE]
== 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/fa/1fay_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1fay ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structures of two crystal forms of the dimeric acidic winged bean agglutinin (WBAII) complexed with methyl-alpha-D-galactose have been determined at 3.0 A and 3.3 A resolution. The subunit structure and dimerisation of the lectin are similar to those of the basic lectin from winged bean (WBAI) and the lectin from Erythrina corallodendron (EcorL). The conformation of a loop and its orientation with respect to the rest of the molecule in WBAII are, however, different from those in all the other legume lectins of known structure. This difference appears to have been caused by the formation of two strategically placed salt bridges in the former. Modelling based on the crystal structures provides a rationale for the specificity of the lectin, which is very different from that of WBAI, for the H-antigenic determinant responsible for O blood group reactivity. It also leads to a qualitative explanation for the thermodynamic data on sugar-binding to the lectin, with special emphasis on the role of a tyrosyl residue in the variable loop in the sugar-binding region in generating the carbohydrate specificity of WBAII.


==About this Structure==
Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin.,Manoj N, Srinivas VR, Surolia A, Vijayan M, Suguna K J Mol Biol. 2000 Oct 6;302(5):1129-37. PMID:11183779<ref>PMID:11183779</ref>
1FAY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus] with AMG, MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FAY OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin., Manoj N, Srinivas VR, Surolia A, Vijayan M, Suguna K, J Mol Biol. 2000 Oct 6;302(5):1129-37. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11183779 11183779]
</div>
<div class="pdbe-citations 1fay" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Psophocarpus tetragonolobus]]
[[Category: Psophocarpus tetragonolobus]]
[[Category: Single protein]]
[[Category: Manoj N]]
[[Category: Manoj, N.]]
[[Category: Srinivas VR]]
[[Category: Srinivas, V.R.]]
[[Category: Suguna K]]
[[Category: Suguna, K.]]
[[Category: Surolia A]]
[[Category: Surolia, A.]]
[[Category: Vijayan M]]
[[Category: Vijayan, M.]]
[[Category: AMG]]
[[Category: CA]]
[[Category: MN]]
[[Category: agglutinin]]
[[Category: glycosylated protein]]
[[Category: h-antigenic specificity]]
[[Category: legume lectin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:34:26 2007''

Latest revision as of 06:37, 30 October 2024

WINGED BEAN ACIDIC LECTIN COMPLEXED WITH METHYL-ALPHA-D-GALACTOSE (MONOCLINIC FORM)

1fay, resolution 3.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA