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1X46

Crystal structure of a hemoglobin component (TA-VII) from Tokunagayusurika akamusi

Summary for 1X46
Entry DOI10.2210/pdb1x46/pdb
Descriptorhemoglobin component VII, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywordshemoglobin, diptera, tokunagayusurika akamusi, midge larva, oxygen storage-transport complex, oxygen storage/transport
Biological sourceTokunagayusurika akamusi
Total number of polymer chains1
Total formula weight17159.07
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 citationKuwada, 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: 17590288
DOI: 10.1016/j.gene.2007.02.049
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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数据于2024-10-30公开中

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