Structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1.9 Å resolution

Pandian Ramesh, S. S. Sundaresan, Pon Sathya Moorthy, Balasubramanian Moovarkumudalvan, M. N. Ponnuswamy

Research output: Contribution to journalArticle

3 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)843-847
Number of pages5
JournalJournal of Synchrotron Radiation
Volume20
Issue number6
DOIs
Publication statusPublished - 1 Nov 2013
Externally publishedYes

Fingerprint

sharks
Hemoglobin
hemoglobin
Synchronous Meteorological Satellite
vertebrates
lungs
homeotherms
amino acids
Amino acids
circulatory system
Tissue
Molecules
water temperature
Polypeptides
polypeptides
Binding sites
breathing
muscles
dioxides
Temperature

Keywords

  • crystal structure
  • haemoglobin
  • heme
  • monoclinic
  • oxygen transport
  • shark
  • tetramer

ASJC Scopus subject areas

  • Instrumentation
  • Nuclear and High Energy Physics
  • Radiation

Cite this

Structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1.9 Å resolution. / Ramesh, Pandian; Sundaresan, S. S.; Sathya Moorthy, Pon; Moovarkumudalvan, Balasubramanian; Ponnuswamy, M. N.

In: Journal of Synchrotron Radiation, Vol. 20, No. 6, 01.11.2013, p. 843-847.

Research output: Contribution to journalArticle

Ramesh, Pandian ; Sundaresan, S. S. ; Sathya Moorthy, Pon ; Moovarkumudalvan, Balasubramanian ; Ponnuswamy, M. N. / Structural studies of haemoglobin from pisces species shortfin mako shark (Isurus oxyrinchus) at 1.9 Å resolution. In: Journal of Synchrotron Radiation. 2013 ; Vol. 20, No. 6. pp. 843-847.
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