4Z8B
crystal structure of a DGL mutant - H51G H131N
Summary for 4Z8B
Entry DOI | 10.2210/pdb4z8b/pdb |
Descriptor | Lectin alpha chain, CALCIUM ION, MANGANESE (II) ION, ... (7 entities in total) |
Functional Keywords | lectin, dioclea grandiflora, h31a-h151n mutant, sugar binding protein |
Biological source | Dioclea grandiflora (Mucana) |
Total number of polymer chains | 1 |
Total formula weight | 26314.10 |
Authors | Zamora-Caballero, S.,Perez, A.,Sanz, L.,Bravo, J.,Calvete, J.J. (deposition date: 2015-04-08, release date: 2015-07-22, Last modification date: 2024-01-10) |
Primary citation | Zamora-Caballero, S.,Perez, A.,Sanz, L.,Bravo, J.,Calvete, J.J. Quaternary structure of Dioclea grandiflora lectin assessed by equilibrium sedimentation and crystallographic analysis of recombinant mutants. Febs Lett., 589:2290-2296, 2015 Cited by PubMed Abstract: The structural basis of the pH dependency of the dimer-tetramer transition exhibited by Brinda's type II Diocleinae lectins was investigated by equilibrium sedimentation and X-ray crystal structure determination of recombinant wild-type and site-directed single and double mutants of the pH-stable tetrameric Dioclea grandiflora lectin (r-αDGL). Releasing the peripheral site interdimeric contact between R60 and D78 rendered a mutant displaying dimer-tetramer equilibrium in the pH range equivalent to pKa±1 of the γ-COOH. Mutation of both histidines 51 and 131, but not the mutation of each His separately, abolished the formation of the Diocleinae canonical tetramer in the pH range 2.5-8.5. The X-ray structure of the double mutant r-αDGL H51G/H131N suggests that H131 plays a crucial role in networking loop 114-125 residues from all four subunits at the central cavity of the tetrameric lectin, and that H51 maintains the central cavity loops in a proper spatial orientation to make H131-mediated interdimer contacts. PubMed: 26226421DOI: 10.1016/j.febslet.2015.07.020 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.951 Å) |
Structure validation
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