1V4U
Crystal structure of bluefin tuna carbonmonoxy-hemoglobin
Summary for 1V4U
| Entry DOI | 10.2210/pdb1v4u/pdb |
| Related | 1V4W 1V4X |
| Descriptor | hemoglobin alpha chain, hemoglobin beta chain, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| Functional Keywords | oxygen transport, heme, respiratory protein, erythrocyte, root effect, swim bladder, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Thunnus thynnus (bluefin tuna) More |
| Total number of polymer chains | 4 |
| Total formula weight | 65943.05 |
| Authors | Yokoyama, T.,Chong, K.T.,Miyazaki, Y.,Nakatsukasa, T.,Unzai, S.,Miyazaki, G.,Morimoto, H.,Jeremy, R.H.T.,Park, S.Y. (deposition date: 2003-11-19, release date: 2004-07-06, Last modification date: 2024-11-06) |
| Primary citation | Yokoyama, T.,Chong, K.T.,Miyazaki, G.,Morimoto, H.,Shih, D.T.,Unzai, S.,Tame, J.R.,Park, S.Y. Novel Mechanisms of pH Sensitivity in Tuna Hemoglobin: A STRUCTURAL EXPLANATION OF THE ROOT EFFECT J.Biol.Chem., 279:28632-28640, 2004 Cited by PubMed Abstract: The crystal structure of hemoglobin has been known for several decades, yet various features of the molecule remain unexplained or controversial. Several animal hemoglobins have properties that cannot be readily explained in terms of their amino acid sequence and known atomic models of hemoglobin. Among these, fish hemoglobins are well known for their widely varying interactions with heterotropic effector molecules and pH sensitivity. Some fish hemoglobins are almost completely insensitive to pH (within physiological limits), whereas others show extremely low oxygen affinity under acid conditions, a phenomenon called the Root effect. X-ray crystal structures of Root effect hemoglobins have not, to date, provided convincing explanations of this effect. Sequence alignments have signally failed to pinpoint the residues involved, and site-directed mutagenesis has not yielded a human hemoglobin variant with this property. We have solved the crystal structure of tuna hemoglobin in the deoxy form at low and moderate pH and in the presence of carbon monoxide at high pH. A comparison of these models shows clear evidence for novel mechanisms of pH-dependent control of ligand affinity. PubMed: 15117955DOI: 10.1074/jbc.M401740200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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