Expression and in silico structural analysis of a rice (Oryza sativa) hemoglobin 5.
This work reports the analysis of an additional hemoglobin (hb) gene copy, hb5, in the genome of rice. The amino acid sequence of Hb5 differs from the previously determined rice Hbs 1-4 in missing 11 residues in helix E. Transcripts of hb5 were found to be ubiquitous in rice organs, and hormone- and stress-response promoters exist upstream of the rice hb5 gene. Furthermore, the modeled structure of Hb5 based on the known crystal structure of rice Hb1 is unusual in that the putative distal His is distant from the heme Fe. This observation suggests that Hb5 binds and releases O(2) easily and thus that it functions as an O(2)-carrier or in some aspects of the O(2) metabolism.
Garrocho-Villegas
Verónica
V
Laboratorio de Biofísica y Biología Molecular, Facultad de Ciencias, Universidad Autónoma del Estado de Morelos, Avenida Universidad 1001, Colonia Chamilpa, 62210 Cuernavaca, Morelos, México.
Bustos-Rivera
Genoveva
G
Gough
Julian
J
Vinogradov
Serge N
SN
Arredondo-Peter
Raúl
R
D000595:Amino Acid Sequence; D001483:Base Sequence; D017931:DNA Primers; D006454:Hemoglobins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012275:Oryza / Q000737:chemistry*; D011487:Protein Conformation; D012333:RNA, Messenger / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D006454:Hemoglobins; D012333:RNA, Messenger