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3S1I

Crystal structure of oxygen-bound hell's gate globin I

Summary for 3S1I
Entry DOI10.2210/pdb3s1i/pdb
Related3S1J
DescriptorHemoglobin-like flavoprotein, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (5 entities in total)
Functional Keywordsglobin, heme, oxygen-bound, autoxidation, oxygen transport, oxygen storage
Biological sourceMethylacidiphilum infernorum (METHYLOKORUS INFERNORUM)
Total number of polymer chains3
Total formula weight50012.39
Authors
Primary citationTeh, A.H.,Saito, J.A.,Baharuddin, A.,Tuckerman, J.R.,Newhouse, J.S.,Kanbe, M.,Newhouse, E.I.,Rahim, R.A.,Favier, F.,Didierjean, C.,Sousa, E.H.S.,Stott, M.B.,Dunfield, P.F.,Gonzalez, G.,Gilles-Gonzalez, M.A.,Najimudin, N.,Alam, M.
Hell's Gate globin I: an acid and thermostable bacterial hemoglobin resembling mammalian neuroglobin
Febs Lett., 585:3250-3258, 2011
Cited by
PubMed Abstract: Hell's Gate globin I (HGbI), a heme-containing protein structurally homologous to mammalian neuroglobins, has been identified from an acidophilic and thermophilic obligate methanotroph, Methylacidiphilum infernorum. HGbI has very high affinity for O(2) and shows barely detectable autoxidation in the pH range of 5.2-8.6 and temperature range of 25-50°C. Examination of the heme pocket by X-ray crystallography and molecular dynamics showed that conformational movements of Tyr29(B10) and Gln50(E7), as well as structural flexibility of the GH loop and H-helix, may play a role in modulating its ligand binding behavior. Bacterial HGbI's unique resistance to the sort of extreme acidity that would extract heme from any other hemoglobin makes it an ideal candidate for comparative structure-function studies of the expanding globin superfamily.
PubMed: 21925500
DOI: 10.1016/j.febslet.2011.09.002
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.77 Å)
Structure validation

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數據於2024-11-13公開中

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