2frf
From Proteopedia
(New page: 200px<br /><applet load="2frf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2frf, resolution 1.20Å" /> '''Horse Heart Myoglobi...) |
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| - | [[Image:2frf.gif|left|200px]]<br /><applet load="2frf" size=" | + | [[Image:2frf.gif|left|200px]]<br /><applet load="2frf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2frf, resolution 1.20Å" /> | caption="2frf, resolution 1.20Å" /> | ||
'''Horse Heart Myoglobin, Nitrite Adduct, Crystal Soak'''<br /> | '''Horse Heart Myoglobin, Nitrite Adduct, Crystal Soak'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nitrite is an important species in the global nitrogen cycle, and the | + | Nitrite is an important species in the global nitrogen cycle, and the nitrite reductase enzymes convert nitrite to nitric oxide (NO). Recently, it has been shown that hemoglobin and myoglobin catalyze the reduction of nitrite to NO under hypoxic conditions. We have determined the 1.20 A resolution crystal structure of the nitrite adduct of ferric horse heart myoglobin (hh Mb). The ligand is bound to iron in the nitrito form, and the complex is formulated as MbIII(ONO-). The Fe-ONO bond length is 1.94 A, and the O-N-O angle is 113 degrees . In addition, the nitrite ligand is stabilized by hydrogen bonding with the distal His64 residue. We have also determined the 1.30 A resolution crystal structures of hh MbIINO. When hh MbIINO is prepared from the reaction of metMbIII with nitrite/dithionite, the FeNO angle is 144 degrees with a Fe-NO bond length of 1.87 A. However, when prepared from the reaction of NO with reduced MbII, the FeNO angle is 120 degrees with a Fe-NO bond length of 2.13 A. This difference in FeNO conformations as a function of preparative method is reproducible, and suggests a role of the distal pocket in hh MbIINO in stabilizing local FeNO conformational minima. |
==About this Structure== | ==About this Structure== | ||
| - | 2FRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with SO4, NO2 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2FRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NO2:'>NO2</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FRF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Copeland, D | + | [[Category: Copeland, D M.]] |
| - | [[Category: Richter-Addo, G | + | [[Category: Richter-Addo, G B.]] |
| - | [[Category: Soares, A | + | [[Category: Soares, A S.]] |
| - | [[Category: West, A | + | [[Category: West, A H.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: NO2]] | [[Category: NO2]] | ||
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[[Category: no2]] | [[Category: no2]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:24:23 2008'' |
Revision as of 15:24, 21 February 2008
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Horse Heart Myoglobin, Nitrite Adduct, Crystal Soak
Overview
Nitrite is an important species in the global nitrogen cycle, and the nitrite reductase enzymes convert nitrite to nitric oxide (NO). Recently, it has been shown that hemoglobin and myoglobin catalyze the reduction of nitrite to NO under hypoxic conditions. We have determined the 1.20 A resolution crystal structure of the nitrite adduct of ferric horse heart myoglobin (hh Mb). The ligand is bound to iron in the nitrito form, and the complex is formulated as MbIII(ONO-). The Fe-ONO bond length is 1.94 A, and the O-N-O angle is 113 degrees . In addition, the nitrite ligand is stabilized by hydrogen bonding with the distal His64 residue. We have also determined the 1.30 A resolution crystal structures of hh MbIINO. When hh MbIINO is prepared from the reaction of metMbIII with nitrite/dithionite, the FeNO angle is 144 degrees with a Fe-NO bond length of 1.87 A. However, when prepared from the reaction of NO with reduced MbII, the FeNO angle is 120 degrees with a Fe-NO bond length of 2.13 A. This difference in FeNO conformations as a function of preparative method is reproducible, and suggests a role of the distal pocket in hh MbIINO in stabilizing local FeNO conformational minima.
About this Structure
2FRF is a Single protein structure of sequence from Equus caballus with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin., Copeland DM, Soares AS, West AH, Richter-Addo GB, J Inorg Biochem. 2006 Aug;100(8):1413-25. Epub 2006 May 5. PMID:16777231
Page seeded by OCA on Thu Feb 21 17:24:23 2008
Categories: Equus caballus | Single protein | Copeland, D M. | Richter-Addo, G B. | Soares, A S. | West, A H. | HEM | NO2 | SO4 | Heme | Iron | Myoglobin | Nitric oxide | Nitrite | No | No2
