8vsh

Crystal structure of Shewanella benthica Group 1 truncated hemoglobin C51S C71S variant with trans heme D

spinqualitylabelsall models 8vsh, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8vsh is a 4 chain structure with sequence from Shewanella benthica KT99. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: A1ADT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A9DF82_9GAMM Publication Abstract from PubMed In our continued investigations of microbial globins, we solved the structure of a truncated hemoglobin from Shewanella benthica, an obligate psychropiezophilic bacterium. The distal side of the heme active site is lined mostly with hydrophobic residues, with the exception of a tyrosine, Tyr34 (CD1) and a histidine, His24 (B13). We found that purified SbHbN, when crystallized in the ferric form with polyethylene glycol as precipitant, turned into a green color over weeks. The electron density obtained from the green crystals accommodated a trans heme d, a chlorin-type derivative featuring a gamma-spirolactone and a vicinal hydroxyl group on a pyrroline ring. In solution, exposure of the protein to one equivalent of hydrogen peroxide resulted in a similar green color change, but caused by the formation of multiple products. These were oxidation species released on protein denaturation, likely including heme d, and a species with heme covalently attached to the polypeptide. The Tyr34Phe replacement prevented the formation of both heme d and the covalent linkage. The ready modification of heme b by SbHbN expands the range of chemistries supported by the globin fold and offers a route to a novel heme cofactor. Heme d formation in a Shewanella benthica hemoglobin.,Martinez Grundman JE, Schultz TD, Schlessman JL, Liu K, Johnson EA, Lecomte JTJ J Inorg Biochem. 2024 Jun 27;259:112654. doi: 10.1016/j.jinorgbio.2024.112654. PMID:38959524 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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