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2olp

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{{STRUCTURE_2olp| PDB=2olp | SCENE= }}
{{STRUCTURE_2olp| PDB=2olp | SCENE= }}
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'''Structure and ligand selection of hemoglobin II from Lucina pectinata'''
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===Structure and ligand selection of hemoglobin II from Lucina pectinata===
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==Overview==
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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) --&gt; 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).
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{{ABSTRACT_PUBMED_18203714}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/18203714 18203714]
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:[http://www.ncbi.nlm.nih.gov/pubmed/18203714 18203714]
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Capillary crystallization and molecular-replacement solution of haemoglobin II from the clam Lucina pectinata., Gavira JA, de Jesus W, Camara-Artigas A, Lopez-Garriga J, Garcia-Ruiz JM, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt, 3):196-9. Epub 2006 Feb 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16511300 16511300]
[[Category: Lucina pectinata]]
[[Category: Lucina pectinata]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Oxygen storage/transport complex]]
[[Category: Oxygen storage/transport complex]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:25:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:40:08 2008''

Revision as of 18:40, 27 July 2008

Image:2olp.png

Template:STRUCTURE 2olp

Structure and ligand selection of hemoglobin II from Lucina pectinata

Template:ABSTRACT PUBMED 18203714

About this Structure

2OLP is a Single protein structure of sequence from Lucina pectinata. Full crystallographic information is available from OCA.

Reference

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

Capillary crystallization and molecular-replacement solution of haemoglobin II from the clam Lucina pectinata., Gavira JA, de Jesus W, Camara-Artigas A, Lopez-Garriga J, Garcia-Ruiz JM, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt, 3):196-9. Epub 2006 Feb 10. PMID:16511300

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