2frf: Difference between revisions
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|PDB= 2frf |SIZE=350|CAPTION= <scene name='initialview01'>2frf</scene>, resolution 1.20Å | |PDB= 2frf |SIZE=350|CAPTION= <scene name='initialview01'>2frf</scene>, resolution 1.20Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2frf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2frf OCA], [http://www.ebi.ac.uk/pdbsum/2frf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2frf RCSB]</span> | |||
}} | }} | ||
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[[Category: Soares, A S.]] | [[Category: Soares, A S.]] | ||
[[Category: West, A H.]] | [[Category: West, A H.]] | ||
[[Category: heme]] | [[Category: heme]] | ||
[[Category: iron]] | [[Category: iron]] | ||
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[[Category: no2]] | [[Category: no2]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:06:43 2008'' | ||
Revision as of 03:06, 31 March 2008
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| , resolution 1.20Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Horse Heart Myoglobin, Nitrite Adduct, Crystal Soak
OverviewOverview
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 StructureAbout this Structure
2FRF is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
ReferenceReference
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
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