6IYH

X-ray sequence and high resolution crystal structure of Persian sturgeon methemoglobin

Replaces:  5JGG

Summary for 6IYH

• Entry DOI: 10.2210/pdb6iyh/pdb
• Related: 5JGG 5JNZ 6IYI
• Descriptor: Alpha chain, Beta chain, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: methemoglobin, heme, iron containing, oxygen-carrying, oxygen binding-transport protein complex, oxygen binding/transport protein
• Biological source: Acipenser persicus; More
• Total number of polymer chains: 2
• Total formula weight: 32537.36

Authors

Seyedarabi, A. (deposition date: 2018-12-16, release date: 2019-04-10, Last modification date: 2023-11-22)

Primary citation

Seyedarabi, A.,Ariaeenejad, S.,Moosavi-Movahedi, A.A.,Rayati, S.,Poursasan, N.,Asiaie, N.,Seraj, Z.,Mehraban, F.,Seyedarabi, S.E.
Novel X-ray sequences and crystal structures of Persian and Starry sturgeon methemoglobins: Highlighting the role of heme pocket waters in causing autoxidation
Biochim Biophys Acta Proteins Proteom, 1867:586-594, 2019

PubMed Abstract: Although there is a high sequence similarity between mammalian and fish hemoglobin (Hb), the oxidation and heme loss rates can vary greatly between them such that fish Hbs oxidise much more rapidly than mammalian Hbs. There is to date no sequence or structural data for any sturgeon Hb to reveal the level of autoxidation in these fish. In this study, novel high resolution X-ray sequences and crystal structures of methemoglobin (Met-Hb) from two sturgeon fish including Persian sturgeon (Acipenser percisus) and Starry sturgeon (Acipenser stellatus) belonging to the Caspian sea has been determined. A comprehensive sequence and structure comparison between these sturgeon Met-Hbs and a number of non-sturgeon and normal and sickle cell anaemia human Hb in varying heme states has been carried out highlighting (i) the structural variability in the heme propionate groups; (ii) the existence of certain residues or their displacement and shift in the heme pocket allowing entry of water molecules into the heme pocket; (iii) the importance of the number of water molecules in the heme pocket; (iv) the hydrogen bonding between oxygens of A and D propionate groups and that of waters in the heme pocket; and (v) the role of heme binding waters causing oxidative stress and heme autoxidation.

PubMed: 30904680
DOI: 10.1016/j.bbapap.2019.03.008

Experimental method

X-RAY DIFFRACTION (1.7 Å)