<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2olp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Revision as of 02:24, 8 February 2016
Structure and ligand selection of hemoglobin II from Lucina pectinata
2olp is a 2 chain structure with sequence from Phacoides pectinatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Lucina pectinata ctenidia harbor three heme proteins: sulfide-reactive hemoglobin I (HbI(Lp)) and the oxygen transporting hemoglobins II and III (HbII(Lp) and HbIII(Lp)) that remain unaffected by the presence of H(2)S. The mechanisms used by these three proteins for their function, including ligand control, remain unknown. The crystal structure of oxygen-bound HbII(Lp) shows a dimeric oxyHbII(Lp) where oxygen is tightly anchored to the heme through hydrogen bonds with Tyr(30)(B10) and Gln(65)(E7). The heme group is buried farther within HbII(Lp) than in HbI(Lp). The proximal His(97)(F8) is hydrogen bonded to a water molecule, which interacts electrostatically with a propionate group, resulting in a Fe-His vibration at 211 cm(-1). The combined effects of the HbII(Lp) small heme pocket, the hydrogen bonding network, the His(97) trans-effect, and the orientation of the oxygen molecule confer stability to the oxy-HbII(Lp) complex. Oxidation of HbI(Lp) Phe(B10) --> Tyr and HbII(Lp) only occurs when the pH is decreased from pH 7.5 to 5.0. Structural and resonance Raman spectroscopy studies suggest that HbII(Lp) oxygen binding and transport to the host bacteria may be regulated by the dynamic displacements of the Gln(65)(E7) and Tyr(30)(B10) pair toward the heme to protect it from changes in the heme oxidation state from Fe(II) to Fe(III).
Structure and ligand selection of hemoglobin II from Lucina pectinata.,Gavira JA, Camara-Artigas A, De Jesus-Bonilla W, Lopez-Garriga J, Lewis A, Pietri R, Yeh SR, Cadilla CL, Garcia-Ruiz JM J Biol Chem. 2008 Apr 4;283(14):9414-23. Epub 2008 Jan 18. PMID:18203714[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Gavira JA, Camara-Artigas A, De Jesus-Bonilla W, Lopez-Garriga J, Lewis A, Pietri R, Yeh SR, Cadilla CL, Garcia-Ruiz JM. Structure and ligand selection of hemoglobin II from Lucina pectinata. J Biol Chem. 2008 Apr 4;283(14):9414-23. Epub 2008 Jan 18. PMID:18203714 doi:https://dx.doi.org/10.1074/jbc.M705026200
