Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A.

by: RF Tilton, ID Kuntz, GA Petsko

Biochemistry, Vol. 23, No. 13. (19 June 1984), pp. 2849-2857.

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xenon

Abstract

X-ray crystallographic data to 1.9-A resolution were collected on sperm whale metmyoglobin equilibrated with 7 atm of xenon gas. The results indicate four xenon sites of occupancy from 0.45 to 1.0. These sites are located in interior spaces or packing defects of the myoglobin molecule. The effects of the bound xenon on the protein structure are minor, and we observe a small overall reduction in refined isotropic atomic protein temperature factors. We interpret the results as a confirmation that, on a time-averaged basis, cavities exist within the myoglobin molecule and suggest that the binding of small ligands in these cavities affects the internal motions and conformational substrates of the protein.

@article{citeulike:3006266, abstract = {X-ray crystallographic data to 1.9-A resolution were collected on sperm whale metmyoglobin equilibrated with 7 atm of xenon gas. The results indicate four xenon sites of occupancy from 0.45 to 1.0. These sites are located in interior spaces or packing defects of the myoglobin molecule. The effects of the bound xenon on the protein structure are minor, and we observe a small overall reduction in refined isotropic atomic protein temperature factors. We interpret the results as a confirmation that, on a time-averaged basis, cavities exist within the myoglobin molecule and suggest that the binding of small ligands in these cavities affects the internal motions and conformational substrates of the protein.}, author = {Tilton, R. F. and Kuntz, I. D. and Petsko, G. A. }, citeulike-article-id = {3006266}, issn = {0006-2960}, journal = {Biochemistry}, keywords = {xenon}, month = {June}, number = {13}, pages = {2849--2857}, posted-at = {2008-07-15 17:07:05}, priority = {2}, title = {Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/6466620}, volume = {23}, year = {1984} }

RIS record

TY - JOUR ID - citeulike:3006266 L3 - citeulike-article-id:3006266 TI - Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A. JF - Biochemistry VL - 23 IS - 13 SP - 2849 EP - 2857 SN - 0006-2960 N2 - X-ray crystallographic data to 1.9-A resolution were collected on sperm whale metmyoglobin equilibrated with 7 atm of xenon gas. The results indicate four xenon sites of occupancy from 0.45 to 1.0. These sites are located in interior spaces or packing defects of the myoglobin molecule. The effects of the bound xenon on the protein structure are minor, and we observe a small overall reduction in refined isotropic atomic protein temperature factors. We interpret the results as a confirmation that, on a time-averaged basis, cavities exist within the myoglobin molecule and suggest that the binding of small ligands in these cavities affects the internal motions and conformational substrates of the protein. KW - xenon AU - Tilton, RF AU - Kuntz, ID AU - Petsko, GA PY - 1984/06/19/ UR - http://view.ncbi.nlm.nih.gov/pubmed/6466620 ER -

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