2pel | pdb_00002pel

PEANUT LECTIN

spinqualitylabelsall models 2pel, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2pel is a 4 chain structure with sequence from Arachis hypogaea. This structure supersedes the now removed PDB entry 1pel. The April 2010 RCSB PDB Molecule of the Month feature on Concanavalin A and Circular Permutation by David Goodsell is 10.2210/rcsb_pdb/mom_2010_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, LAT, LBT, MN 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. Publication Abstract from PubMed The structure of the complex of the tetrameric peanut lectin with lactose has been refined to an R-value of 16.4% using 2.25 angstroms resolution X-ray diffraction data. The subunit conformation in the structure is similar to that in other legume lectins except in the loops. It has been shown that in the tertiary structure of legume lectins, the short five-stranded sheet plays a major role in connecting the larger flat six-stranded and curved seven-stranded sheets. Furthermore, the loops that connect the strands at the two ends of the seven-stranded sheet curve toward and interact with each other to produce a second hydrophobic core in addition to the one between the two large sheets. The protein-lactose interactions involve the invariant features observed in other legume lectins in addition to those characteristic of peanut lectin. The "open" quaternary association in peanut lectin is stabilised by hydrophobic, hydrogen-bonded and water-mediated interactions. Contrary to the earlier belief, the structure of peanut lectin demonstrates that the variability in quaternary association in legume lectins, despite all of them having nearly the same tertiary structure, is not necessarily caused by covalently bound carbohydrate. An attempt has been made to provide a structural rationale for this variability, on the basis of buried surface areas during dimerisation. A total of 45 water molecules remain invariant when the hydration shells of the four subunits are compared. A majority of them appear to be involved in stabilising loops. Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex.,Banerjee R, Das K, Ravishankar R, Suguna K, Surolia A, Vijayan M J Mol Biol. 1996 Jun 7;259(2):281-96. PMID:8656429 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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