1X46
Crystal structure of a hemoglobin component (TA-VII) from Tokunagayusurika akamusi
Summary for 1X46
Entry DOI | 10.2210/pdb1x46/pdb |
Descriptor | hemoglobin component VII, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
Functional Keywords | hemoglobin, diptera, tokunagayusurika akamusi, midge larva, oxygen storage-transport complex, oxygen storage/transport |
Biological source | Tokunagayusurika akamusi |
Total number of polymer chains | 1 |
Total formula weight | 17159.07 |
Authors | Kuwada, T.,Hasegawa, T.,Sato, S.,Sato, I.,Ishikawa, K.,Takagi, T.,Shishikura, F. (deposition date: 2005-05-14, release date: 2005-05-24, Last modification date: 2024-03-13) |
Primary citation | Kuwada, T.,Hasegawa, T.,Sato, S.,Sato, I.,Ishikawa, K.,Takagi, T.,Shishikura, F. Crystal structures of two hemoglobin components from the midge larva Propsilocerus akamusi (Orthocladiinae, Diptera). Gene, 398:29-34, 2007 Cited by PubMed Abstract: The polymorphic components of hemoglobin (Hb) of the midge larva Propsilocerus akamusi were classified into two distinct types dependent on their spectroscopic properties, normal absorption (N) and low absorption (L). Analyses of the amino acid sequences of component VII (N-type Hb) and component V (L-type Hb) from P. akamusi indicated that one remarkable difference is the replacement of the distal histidine (His) with isoleucine (Ile) in component V. To clarify the structural differences between the two Hb components, we determined the crystal structures of components V and VII at resolutions of 1.64 A and 1.50 A, respectively. These crystal structures indicated a short additional helix comprising three amino acid residues at the C-terminal region in component V, and a typical globin fold including eight helices in component VII. Comparison of the heme regions of the Hb components suggests that the structural changes of the heme region in component V on ligation differ from that of usual Hb. PubMed: 17590288DOI: 10.1016/j.gene.2007.02.049 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
Download full validation report