1QI8
DEOXYGENATED STRUCTURE OF A DISTAL POCKET HEMOGLOBIN MUTANT
Summary for 1QI8
| Entry DOI | 10.2210/pdb1qi8/pdb |
| Descriptor | HEMOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | hemoglobin, blood substitute, low no reactivity, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 64835.31 |
| Authors | Miele, A.E.,Vallone, B.,Santanche, S.,Travaglini-Allocatelli, C.,Bellelli, A.,Brunori, M. (deposition date: 1999-06-07, release date: 1999-07-11, Last modification date: 2023-08-16) |
| Primary citation | Miele, A.E.,Santanche, S.,Travaglini-Allocatelli, C.,Vallone, B.,Brunori, M.,Bellelli, A. Modulation of ligand binding in engineered human hemoglobin distal pocket. J.Mol.Biol., 290:515-524, 1999 Cited by PubMed Abstract: Functional and structural studies on hemoglobin and myoglobin from different animals and engineered variants have enlightened the great importance of the physico-chemical properties of the side-chains at topological position B10 and E7. These residues proved to be crucial to the discrimination and stabilisation of gaseous ligands. In view of the data obtained on the high oxygen affinity hemoglobin from Ascaris worms and a new mutant of sperm whale myoglobin, we selected the two mutations Leu B10-->Tyr and His E7-->Gln as potentially relevant to control ligand binding parameters in the alpha and beta-chains of human hemoglobin. Here, we present an investigation of three new mutants: HbalphaYQ (alpha2YQbeta2A), HbbetaYQ (alpha2Abeta2YQ) and HbalphabetaYQ (alpha2YQbeta2YQ). They are characterised by a very low reactivity for NO, O2 and CO, and a reduced cooperativity. Their functional properties are not inconsistent with the behaviour expected for a two-state allosteric model. Proteins with these substitutions may be considered as candidates for the synthesis of a possible "blood substitute", which should yield an O2 adduct stable to autoxidation and slowly reacting with NO. The mutant HbalphabetaYQ is particularly interesting because the rate of reaction of NO with the oxy and deoxy derivatives is reduced. A structural interpretation of our data is presented based on the 3D structure of deoxy HbalphabetaYQ determined by crystallography at 1.8 A resolution. PubMed: 10390349DOI: 10.1006/jmbi.1999.2869 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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