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

Overview

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.

publication date

  • June 19, 1984

Research

keywords

  • Hemeproteins
  • Metmyoglobin
  • Xenon

Identity

Scopus Document Identifier

  • 0021766921

Digital Object Identifier (DOI)

  • 10.1021/bi00308a002

PubMed ID

  • 6466620

Additional Document Info

volume

  • 23

issue

  • 13