Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/104969
Title: Structure of liganded T-state haemoglobin from cat ( Felis silvestris catus ), a low oxygen-affinity species, in two different crystal forms
Authors: Balasubramanian, Moovarkumudalvan
Sathya Moorthy, Ponnuraj
Neelagandan, Kamariah
Ramadoss, Ramya
Kolatkar, Prasanna R.
Ponnuswamy, M. N.
Keywords: DRNTU::Science::Biological sciences::Molecular biology
Issue Date: 2014
Source: Balasubramanian, M., Sathya Moorthy, P., Neelagandan, K., Ramadoss, R., Kolatkar, P. R., & Ponnuswamy, M. N. (2014). Structure of liganded T-state haemoglobin from cat ( Felis silvestris catus ), a low oxygen-affinity species, in two different crystal forms . Acta Crystallographica Section D Biological Crystallography, 70(7), 1898-1906.
Series/Report no.: Acta crystallographica section D biological crystallography
Abstract: Haemoglobin (Hb) is an iron-containing metalloprotein which plays a major role in the transportation of oxygen from the lungs to tissues and of carbon dioxide back to the lungs. Hb is in equilibrium between low-affinity tense (T) and high-affinity relaxed (R) states associated with its unliganded and liganded forms, respectively. Mammalian species can be classified into two groups on the basis of whether they express `high' or `low' oxygen-affinity Hbs. Although Hbs from the former group have been studied extensively, a more limited number of structural studies have been performed for low oxygen-affinity Hbs. Here, the crystal structure of low oxygen-affinity cat methaemoglobin (metHb) has been solved at 2.0 and 2.4 Å resolution in two different crystal forms. Even though both structures are fully liganded, they unusually adopt a T-state-like quaternary conformation but with several localized R-like tertiary-structural and quaternary-structural features. The study provides atomic-level insights into the ligand-binding properties of this Hb, including its low cooperativity, blunt response to allosteric effectors and low affinity for oxygen, as well as further contributing to the mechanism underlying Hb allostery.
URI: https://hdl.handle.net/10356/104969
http://hdl.handle.net/10220/20378
ISSN: 1399-0047
DOI: 10.1107/S139900471400916X
Rights: © 2014 International Union of Crystallography. This paper was published in Acta Crystallographica Section D Biological Crystallography and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [http://dx.doi.org/10.1107/S139900471400916X].  One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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