Bioinformatic characterization of Lucina pectinata hemoglobins (778.9)
نویسندگان
چکیده
منابع مشابه
Crystallization of hemoglobins II and III of the symbiont-harboring clam Lucina pectinata.
Diffraction data to 2.7 A resolution were measured on crystals of the homotetramers of components II and III of the cytoplasmic hemoglobin of the symbiont-harboring clam Lucina pectinata. Even though the crystallization conditions are different and the sequence homology of the two hemoglobins is only 63%, the crystals are isomorphous to each other and to the heterotetramer Hb II/III, implying t...
متن کاملStructure and ligand selection of hemoglobin II from Lucina pectinata.
Lucina pectinata ctenidia harbor three heme proteins: sulfide-reactive hemoglobin I (HbI(Lp)) and the oxygen transporting hemoglobins II and III (HbII(Lp) and HbIII(Lp)) that remain unaffected by the presence of H(2)S. The mechanisms used by these three proteins for their function, including ligand control, remain unknown. The crystal structure of oxygen-bound HbII(Lp) shows a dimeric oxyHbII(L...
متن کاملExpression and purification of recombinant hemoglobin I from Lucina pectinata.
Hemoglobin I (HbI) from Lucina pectinata reacts with hydrogen sulfide to form the ferric sulfide complex needed to transport H2S to the bacterial endosymbiont. To further study HbI, expression studies of this protein were performed in Escherichia coli. This is the first time that the recombinant HbI was produced using a recombinant DNA expression system. Hemoglobin I cDNA was amplified and clon...
متن کاملCharacterization and Expression of the Lucina pectinata Oxygen and Sulfide Binding Hemoglobin Genes
The clam Lucina pectinata lives in sulfide-rich muds and houses intracellular symbiotic bacteria that need to be supplied with hydrogen sulfide and oxygen. This clam possesses three hemoglobins: hemoglobin I (HbI), a sulfide-reactive protein, and hemoglobin II (HbII) and III (HbIII), which are oxygen-reactive. We characterized the complete gene sequence and promoter regions for the oxygen react...
متن کاملEffects of active site mutations in haemoglobin I from Lucina pectinata: a molecular dynamic study
Haemoglobin I from Lucina pectinata is a monomeric protein consisting of 142 amino acids. Its active site contains a peculiar arrangement of phenylalanine residues (PheB10, PheCD1 and PheE11) and a distal Gln at position E7. Active site mutations at positions B10, E7 and E11 were performed in deoxy haemoglobin I (HbI), followed by 10 ns molecular dynamic simulations. The results showed that the...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2014
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.28.1_supplement.778.9