2DC3

Crystal structure of human cytoglobin at 1.68 angstroms resolution

Summary for 2DC3

• Entry DOI: 10.2210/pdb2dc3/pdb
• Descriptor: Cytoglobin, PROTOPORPHYRIN IX CONTAINING FE, ACETIC ACID, ... (4 entities in total)
• Functional Keywords: cytoglobin, myoglobin, heme, oxygen transport, oxygen storage, riken structural genomics/proteomics initiative, rsgi, structural genomics, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q8WWM9
• Total number of polymer chains: 2
• Total formula weight: 44724.81

Authors

Makino, M.,Sugimoto, H.,Sawai, H.,Kawada, N.,Yoshizato, K.,Shiro, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-12-21, release date: 2006-05-23, Last modification date: 2023-10-25)

Primary citation

Makino, M.,Sugimoto, H.,Sawai, H.,Kawada, N.,Yoshizato, K.,Shiro, Y.
High-resolution structure of human cytoglobin: identification of extra N- and C-termini and a new dimerization mode.
Acta Crystallogr.,Sect.D, 62:671-677, 2006

PubMed Abstract: Cytoglobin (Cgb) is a recently discovered member of the vertebrate haem-containing globin family. The structure of a new crystal form of wild-type human Cgb (space group C2) was determined at a resolution of 1.68 Angstrom. The results show the presence of an additional helix in the N-terminal residues (4-20) prior to the A helix and an ordered loop structure in the C-terminal region (168-188), while these extended peptides were invisible owing to disorder in the previously reported structures using a P3(2)21 crystal at a resolution of 2.4 Angstrom. A detailed comparison of the two crystal structures shows differences in the conformation of the residues (i.e. Arg84) in the haem environment owing to a different dimeric arrangement.

PubMed: 16699195
DOI: 10.1107/S0907444906013813

Experimental method

X-RAY DIFFRACTION (1.68 Å)