2mm1

From Proteopedia

X-RAY CRYSTAL STRUCTURE OF A RECOMBINANT HUMAN MYOGLOBIN MUTANT AT 2.8 ANGSTROMS RESOLUTION

Overview

We have grown crystals in trigonal space group P3(2)21 of a mutant human, myoglobin, aquomet form, in which lysine at position 45 has been replaced, by arginine and cysteine at position 110 has been replaced by alanine., Suitable crystals of native recombinant human myoglobin have not been, obtained. We have used the molecular replacement method to determine the, X-ray crystal structure of the mutant at 2.8 A resolution. At the present, stage of refinement, the crystallographic R-value for the model, with, tightly restrained stereochemistry, is 0.158 for 5.0 to 2.8 A data. As, expected, the overall structure is quite similar to the sperm whale, myoglobin structure. Arginine 45 adopts a well-ordered conformation, similar to that found in aquomet sperm whale myoglobin.

Disease

Known diseases associated with this structure: Chronic infections, due to MBL deficiency OMIM:[154545], Diabetes mellitus, gestational, susceptibility to OMIM:[154545], Mannose-binding protein deficiency OMIM:[154545], Meningococcal disease, susceptibility to OMIM:[154545]

About this Structure

2MM1 is a Single protein structure of sequence from Homo sapiens with HEM as ligand. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure of a recombinant human myoglobin mutant at 2.8 A resolution., Hubbard SR, Hendrickson WA, Lambright DG, Boxer SG, J Mol Biol. 1990 May 20;213(2):215-8. PMID:2342104

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