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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 213 215-8 (1990)
Cited: 47 times
EuropePMC logo PMID: 2342104

Abstract

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crystals in trigonal space group P3(2)21 of a mutant human myoglobin, aquomet form, in which lysine at position 45 has been replaced by arginine and cysteine at position 110 has been replaced by alanine.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.

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  5. Allosteric modulation by S-nitrosation in the low-O₂ affinity myoglobin from rainbow trout. Helbo S, Fago A. Am J Physiol Regul Integr Comp Physiol 300 R101-8 (2011)
  6. Myocyte specific overexpression of myoglobin impairs angiogenesis after hind-limb ischemia. Hazarika S, Angelo M, Li Y, Aldrich AJ, Odronic SI, Yan Z, Stamler JS, Annex BH. Arterioscler Thromb Vasc Biol 28 2144-2150 (2008)
  7. Neuroglobin and cytoglobin: Two new entries in the hemoglobin superfamily*. Ascenzi P, Bocedi A, de Sanctis D, Pesce A, Bolognesi M, Marden MC, Dewilde S, Moens L, Hankeln T, Burmester T. Biochem Mol Biol Educ 32 305-313 (2004)
  8. Myoglobin maturation is driven by the hsp90 chaperone machinery and by soluble guanylyl cyclase. Ghosh A, Dai Y, Biswas P, Stuehr DJ. FASEB J 33 9885-9896 (2019)
  9. Perturbations of the distal heme pocket in human myoglobin mutants probed by infrared spectroscopy of bound CO: correlation with ligand binding kinetics. Balasubramanian S, Lambright DG, Boxer SG. Proc Natl Acad Sci U S A 90 4718-4722 (1993)
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  17. Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 A resolution. Shirai T, Fujikake M, Yamane T, Inaba K, Ishimori K, Morishima I. J Mol Biol 287 369-382 (1999)
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  19. On the Need to Develop Guidelines for Characterizing and Reporting Intrinsic Disorder in Proteins. Vincent M, Uversky VN, Schnell S. Proteomics 19 e1800415 (2019)
  20. Dynamical comparison between myoglobin and hemoglobin. Aharoni R, Tobi D. Proteins 86 1176-1183 (2018)
  21. Myoglobin modification by enzyme-generated dopamine reactive species. Nicolis S, Zucchelli M, Monzani E, Casella L. Chemistry 14 8661-8673 (2008)


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