1SDL

CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A

Summary for 1SDL

• Entry DOI: 10.2210/pdb1sdl/pdb
• Descriptor: HEMOGLOBIN A, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (6 entities in total)
• Functional Keywords: heme, oxygen transport, respiratory protein, erythrocyte, disease mutation, polymorphism, acetylation
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 64869.23

Authors

Schumacher, M.A.,Dixon, M.M.,Kluger, R.,Jones, R.T.,Brennan, R.G. (deposition date: 1996-02-26, release date: 1996-08-01, Last modification date: 2024-06-05)

Primary citation

Schumacher, M.A.,Dixon, M.M.,Kluger, R.,Jones, R.T.,Brennan, R.G.
Allosteric transition intermediates modelled by crosslinked haemoglobins.
Nature, 375:84-87, 1995

PubMed Abstract: The structural end-points of haemoglobin's transition from its low-oxygen-affinity (T) to high-oxygen-affinity (R) state, have been well established by X-ray crystallography, but short-lived intermediates have proved less amenable to X-ray studies. Here we use chemical crosslinking to fix these intermediates for structural characterization. We describe the X-ray structures of three haemoglobins, alpha 2 beta 1S82 beta, alpha 2 beta 1Tm82 beta and alpha 2 beta 1,82Tm82 beta, which were crosslinked between the amino groups of residues beta Val1 and beta Lys82 by 3,3'-stilbenedicarboxylic acid (S) or trimesic acid (Tm) while in the deoxy state, and saturated with carbon monoxide before crystallization. alpha 2 beta 1S82 beta, which has almost normal oxygen affinity, is completely in the R-state conformation; however, alpha 2 beta 1Tm82 beta and alpha 2 beta 1,82Tm82 beta, both of which have low oxygen affinity, have been prevented from completing their transition into the R state and display many features of a transitional intermediate. These haemoglobins therefore represent a snapshot of the nascent R state.

PubMed: 7723849
DOI: 10.1038/375084a0

Experimental method

X-RAY DIFFRACTION (1.8 Å)