5c6e

Joint X-ray/neutron structure of equine cyanomet hemoglobin in R state

spinqualitylabelsall models 5c6e, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c6e is a 2 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CYN, DOD, HEM Related: 5c8i, 5ccd Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HBA_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues. [HBB_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues. Publication Abstract from PubMed Neutron crystallography provides direct visual evidence of the atomic positions of deuterium-exchanged H atoms, enabling the accurate determination of the protonation/deuteration state of hydrated biomolecules. Comparison of two neutron structures of hemoglobins, human deoxyhemoglobin (T state) and equine cyanomethemoglobin (R state), offers a direct observation of histidine residues that are likely to contribute to the Bohr effect. Previous studies have shown that the T-state N-terminal and C-terminal salt bridges appear to have a partial instead of a primary overall contribution. Four conserved histidine residues [alphaHis72(EF1), alphaHis103(G10), alphaHis89(FG1), alphaHis112(G19) and betaHis97(FG4)] can become protonated/deuterated from the R to the T state, while two histidine residues [alphaHis20(B1) and betaHis117(G19)] can lose a proton/deuteron. alphaHis103(G10), located in the alpha1:beta1 dimer interface, appears to be a Bohr group that undergoes structural changes: in the R state it is singly protonated/deuterated and hydrogen-bonded through a water network to betaAsn108(G10) and in the T state it is doubly protonated/deuterated with the network uncoupled. The very long-term H/D exchange of the amide protons identifies regions that are accessible to exchange as well as regions that are impermeable to exchange. The liganded relaxed state (R state) has comparable levels of exchange (17.1% non-exchanged) compared with the deoxy tense state (T state; 11.8% non-exchanged). Interestingly, the regions of non-exchanged protons shift from the tetramer interfaces in the T-state interface (alpha1:beta2 and alpha2:beta1) to the cores of the individual monomers and to the dimer interfaces (alpha1:beta1 and alpha2:beta2) in the R state. The comparison of regions of stability in the two states allows a visualization of the conservation of fold energy necessary for ligand binding and release. Visualizing the Bohr effect in hemoglobin: neutron structure of equine cyanomethemoglobin in the R state and comparison with human deoxyhemoglobin in the T state.,Dajnowicz S, Seaver S, Hanson BL, Fisher SZ, Langan P, Kovalevsky AY, Mueser TC Acta Crystallogr D Struct Biol. 2016 Jul 1;72(Pt 7):892-903. doi:, 10.1107/S2059798316009049. Epub 2016 Jun 28. PMID:27377386 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemoglobin 3D structures

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