2dh1
From Proteopedia
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'''Crystal structure of peanut lectin lactose-azobenzene-4,4'-dicarboxylic acid-lactose complex''' | '''Crystal structure of peanut lectin lactose-azobenzene-4,4'-dicarboxylic acid-lactose complex''' | ||
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[[Category: Surolia, A.]] | [[Category: Surolia, A.]] | ||
[[Category: Vijayan, M.]] | [[Category: Vijayan, M.]] | ||
| - | [[Category: | + | [[Category: Agglutinin]] |
| - | [[Category: | + | [[Category: Carbohydrate specificity]] |
| - | [[Category: | + | [[Category: Crosslink]] |
| - | [[Category: | + | [[Category: Legume lectin]] |
| - | [[Category: | + | [[Category: Multivalency]] |
| - | [[Category: | + | [[Category: Open quaternary structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:24:36 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:24, 3 May 2008
Crystal structure of peanut lectin lactose-azobenzene-4,4'-dicarboxylic acid-lactose complex
Overview
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.
About this Structure
2DH1 is a Single protein structure of sequence from Arachis hypogaea. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 00:24:36 2008
