2c0k
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2c0k.gif|left|200px]] | [[Image:2c0k.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2c0k", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_2c0k| PDB=2c0k | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''THE STRUCTURE OF HEMOGLOBIN FROM THE BOTFLY GASTEROPHILUS INTESTINALIS''' | '''THE STRUCTURE OF HEMOGLOBIN FROM THE BOTFLY GASTEROPHILUS INTESTINALIS''' | ||
| Line 32: | Line 29: | ||
[[Category: Nardini, M.]] | [[Category: Nardini, M.]] | ||
[[Category: Pesce, A.]] | [[Category: Pesce, A.]] | ||
| - | [[Category: | + | [[Category: Gasterophilus intestinalis hemoglobin]] |
| - | [[Category: | + | [[Category: Heme]] |
| - | [[Category: | + | [[Category: Insect hemoglobin]] |
| - | [[Category: | + | [[Category: Iron]] |
| - | [[Category: | + | [[Category: Metal-binding]] |
| - | [[Category: | + | [[Category: Oxygen transport]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:03:35 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:03, 3 May 2008
THE STRUCTURE OF HEMOGLOBIN FROM THE BOTFLY GASTEROPHILUS INTESTINALIS
Overview
Hemoglobins (Hbs) reversibly bind gaseous diatomic ligands (e.g., O2) as the sixth heme axial ligand of the penta-coordinate deoxygenated form. Selected members of the Hb superfamily, however, display a functionally relevant hexa-coordinate heme Fe atom in their deoxygenated state. Endogenous heme hexa-coordination is generally provided in these Hbs by the E7 residue (often His), which thus modulates accessibility to the heme distal pocket and reactivity of the heme toward exogenous ligands. Such a pivotal role of the E7 residue is prominently shown by analysis of the functional and structural properties of insect Hbs. Here, we report the 2.6 A crystal structure of oxygenated Gasterophilus intestinalis Hb1, a Hb known to display a penta-coordinate heme in the deoxygenated form. The structure is analyzed in comparison with those of Drosophila melanogaster Hb, exhibiting a hexa-coordinate heme in its deoxygenated derivative, and of Chironomus thummi thummi HbIII, which displays a penta-coordinate heme in the deoxygenated form. Despite evident structural differences in the heme distal pockets, the distinct molecular mechanisms regulating O2 binding to the three insect Hbs result in similar O(2 affinities (P50 values ranging between 0.12 torr and 0.46 torr).
About this Structure
2C0K is a Single protein structure of sequence from Gasterophilus intestinalis. Full crystallographic information is available from OCA.
Reference
Modulation of oxygen binding to insect hemoglobins: the structure of hemoglobin from the botfly Gasterophilus intestinalis., Pesce A, Nardini M, Dewilde S, Hoogewijs D, Ascenzi P, Moens L, Bolognesi M, Protein Sci. 2005 Dec;14(12):3057-63. Epub 2005 Oct 31. PMID:16260762 Page seeded by OCA on Sat May 3 21:03:35 2008
