3MKB

Crystal structure determination of Shortfin Mako (Isurus oxyrinchus) hemoglobin at 1.9 Angstrom resolution

Summary for 3MKB

• Entry DOI: 10.2210/pdb3mkb/pdb
• Related: 1gcv 1gcw
• Descriptor: Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• Functional Keywords: hemoglobin, oxygen affinity, isurus oxyrinchus, shortfin mako, oxygen storage, oxygen transport
• Biological source: Isurus oxyrinchus (Shortfin mako shark); More
• Total number of polymer chains: 4
• Total formula weight: 62718.81

Authors

Ramesh, P.,Sundaresan, S.S.,Sathya Moorthy, P.,Balasubramanian, M.,Ponnuswamy, M.N. (deposition date: 2010-04-14, release date: 2011-01-26, Last modification date: 2023-11-01)

Primary citation

Ramesh, P.,Sundaresan, S.S.,Sathya Moorthy, P.,Balasubramanian, M.,Ponnuswamy, M.N.
Structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1.9 angstrom resolution
J.SYNCHROTRON RADIAT., 20:843-847, 2013

PubMed Abstract: Haemoglobin (Hb) is a tetrameric iron-containing protein that carries oxygen from the lungs to tissues and carbon dioxide from tissues back to the lungs. Pisces are the advanced aquatic vertebrates capable of surviving at wide depth ranges. The shortfin mako shark (SMS) is the pelagic, largest, fastest and most sophisticated species of the shark kingdom with well developed eyes. Mostly the pisces species are cold blooded in nature. Distinctly, the SMSs are warm-blooded animals with an advanced circulatory system. SMSs are capable of maintaining elevated muscle temperatures up to 33 K above the ambient water temperatures at a depth of 150-500 m. SMSs have a diverged air-breathing mechanism compared with other vertebrates. The haemoglobin molecule consists of four polypeptide chains, namely two α chains, each with 140 amino acids and two β chains each having 136 amino acids. The SMS Hb was found to crystallize in monoclinic space group P21 using the hanging-drop vapour-diffusion method at room temperature. The crystal packing parameters for the SMS Hb structure contain one whole biological molecule in the asymmetric unit with a solvent content of 47%. The SMS Hb quaternary structural features interface-interface interactions and heme binding sites are discussed with different state Hbs and the results reveal that SMS Hb adopts an unliganded deoxy T state conformation.

PubMed: 24121325
DOI: 10.1107/S0909049513021572

Experimental method

X-RAY DIFFRACTION (1.9 Å)