5lfg

X-ray structure of a new fully ligated carbomonoxy form of Trematomus newnesi hemoglobin (Hb1TnCO).

spinqualitylabelsall models 5lfg, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lfg is a 4 chain structure with sequence from Trematomus newnesi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.94Å Ligands: ACE, CMO, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HBA1_TRENE Publication Abstract from PubMed Although the end points of the functional transitions of tetrameric hemoglobins (Hbs) have been well characterized, atomic-resolution data on R-T intermediate states are extremely limited. Herein, the X-ray structures of two independent tetramers of the fully ligated carbomonoxy form of Trematomus newnesi hemoglobin (Hb1Tn) within the same crystal are described. These structures show peculiar features in the heme pocket, EF corner, and tertiary/quaternary structure. Distal histidine side chains have a propensity to swing out of the heme pocket and thus allow compression of the EF corner. In this rotameric state, the distal His group does not interact with the CO ligand, consistent with FTIR spectra recorded in solution. At the quaternary-structure level, one tetramer is an intermediate R-T state, whereas the other assumes a T-like structure. Altogether, the structures of these tetramers provide the best available atomic-level picture of the R-->T transition of vertebrate Hbs. Fine Sampling of the R-->T Quaternary-Structure Transition of a Tetrameric Hemoglobin.,Vitagliano L, Mazzarella L, Merlino A, Vergara A Chemistry. 2017 Jan 12;23(3):605-613. doi: 10.1002/chem.201603421. Epub 2016 Dec , 7. PMID:27808442 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemoglobin 3D structures

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