2dh1: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2dh1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DH1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2dh1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DH1 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pel|2pel]], [[2tep|2tep]], [[1v6i|1v6i]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 7.65&#8491;</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=2dh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dh1 OCA], [https://pdbe.org/2dh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dh1 RCSB], [https://www.ebi.ac.uk/pdbsum/2dh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dh1 ProSAT]</span></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=2dh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dh1 OCA], [https://pdbe.org/2dh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dh1 RCSB], [https://www.ebi.ac.uk/pdbsum/2dh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dh1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/LECG_ARAHY LECG_ARAHY]] D-galactose specific lectin.  
[https://www.uniprot.org/uniprot/LECG_ARAHY LECG_ARAHY] D-galactose specific lectin.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2dh1 ConSurf].
</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=2dh1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The x-ray crystal structure of the tetrameric T-antigen-binding lectin from peanut, M(r) 110,000, has been determined by using the multiple isomorphous replacement method and refined to an R value of 0.218 for 22,155 reflections within the 10- to 2.95-A resolution range. Each subunit has essentially the same characteristic tertiary fold that is found in other legume lectins. The structure, however, exhibits an unusual quaternary arrangement of subunits. Unlike other well-characterized tetrameric proteins with identical subunits, peanut lectin has neither 222 (D2) nor fourfold (C4) symmetry. A noncrystallographic twofold axis relates two halves of the molecule. The two monomers in each half are related by a local twofold axis. The mutual disposition of the axes is such that they do not lead to a closed point group. Furthermore, the structure of peanut lectin demonstrates that differences in subunit arrangement in legume lectins could be due to factors intrinsic to the protein molecule and, contrary to earlier suggestions, are not necessarily caused by interactions involving covalently linked sugar. The structure provides a useful framework for exploring the structural basis and the functional implications of the variability in the subunit arrangement in legume lectins despite all of them having nearly the same subunit structure, and also for investigating the general problem of "open" quaternary assembly in oligomeric proteins.
Crystal structure of peanut lectin, a protein with an unusual quaternary structure.,Banerjee R, Mande SC, Ganesh V, Das K, Dhanaraj V, Mahanta SK, Suguna K, Surolia A, Vijayan M Proc Natl Acad Sci U S A. 1994 Jan 4;91(1):227-31. PMID:8278370<ref>PMID:8278370</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2dh1" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Galactose-binding lectin|Galactose-binding lectin]]
*[[Galactose-binding lectin|Galactose-binding lectin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arachis hypogaea]]
[[Category: Arachis hypogaea]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Jayaraman, N]]
[[Category: Jayaraman N]]
[[Category: Natchiar, S K]]
[[Category: Natchiar SK]]
[[Category: Nivedita, M]]
[[Category: Nivedita M]]
[[Category: Sagarika, D]]
[[Category: Sagarika D]]
[[Category: Srinivas, O]]
[[Category: Srinivas O]]
[[Category: Surolia, A]]
[[Category: Surolia A]]
[[Category: Vijayan, M]]
[[Category: Vijayan M]]
[[Category: Agglutinin]]
[[Category: Carbohydrate specificity]]
[[Category: Crosslink]]
[[Category: Legume lectin]]
[[Category: Multivalency]]
[[Category: Open quaternary structure]]
[[Category: Sugar binding protein]]

Latest revision as of 11:26, 25 October 2023

Crystal structure of peanut lectin lactose-azobenzene-4,4'-dicarboxylic acid-lactose complexCrystal structure of peanut lectin lactose-azobenzene-4,4'-dicarboxylic acid-lactose complex

Structural highlights

2dh1 is a 4 chain structure with sequence from Arachis hypogaea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 7.65Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LECG_ARAHY D-galactose 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

2dh1, resolution 7.65Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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