1CH4

MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V)

Summary for 1CH4

• Entry DOI: 10.2210/pdb1ch4/pdb
• Descriptor: MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (4 entities in total)
• Functional Keywords: oxygen transport, chimera protein, respiratory protein, heme
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 4
• Total formula weight: 65826.90

Authors

Shirai, T.,Fujikake, M.,Yamane, T.,Inaba, K.,Ishimori, K.,Morishima, I. (deposition date: 1998-06-11, release date: 1999-04-27, Last modification date: 2024-04-03)

Primary citation

Shirai, T.,Fujikake, M.,Yamane, T.,Inaba, K.,Ishimori, K.,Morishima, I.
Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 A resolution.
J.Mol.Biol., 287:369-382, 1999

PubMed Abstract: The crystal structure of the homotetramer of a chimera beta alpha-subunit of human hemoglobin was refined at 2.5 A resolution. The chimera subunit was constructed by replacing an exon-encoded module M4 of the beta-subunit with that of the alpha-subunit, simulating an exon-shuffling event. The implanted module M4 retained the native alpha-subunit structure, while module M3 was disturbed around the site where a new type of intron was recently found. Some of the residues were found in alternative conformations that avoid steric hindrance at the subunit interface. The modules are modestly rigid in their backbone structures by using side-chains to compensate for interface incompatibility.

PubMed: 10080899
DOI: 10.1006/jmbi.1999.2603

Experimental method

X-RAY DIFFRACTION (2.5 Å)