1jdo: Difference between revisions
New page: left|200px<br /><applet load="1jdo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdo, resolution 1.90Å" /> '''SPERM WHALE MYOGLOBI... |
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[[Image:1jdo.gif|left|200px]]<br /><applet load="1jdo" size=" | [[Image:1jdo.gif|left|200px]]<br /><applet load="1jdo" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jdo, resolution 1.90Å" /> | caption="1jdo, resolution 1.90Å" /> | ||
'''SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)'''<br /> | '''SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of the ferrous nitric oxide form of native sperm whale | The structure of the ferrous nitric oxide form of native sperm whale myoglobin has been determined by X-ray crystallography to 1.7 angstroms resolution. The nitric oxide ligand is bent with respect to the heme plane: the Fe-N-O angle is 112 degrees. This angle is smaller than those observed in model compounds and in lupin leghemoglobin. The exact angle appears to be influenced by the strength of the proximal bond and hydrogen bonding interactions between the distal histidine and the bound ligand. Specifically, the N(epsilon) atom of histidine64 is located 2.8 angstroms away from the nitrogen atom of the bound ligand, implying electrostatic stabilization of the FeNO complex. This interpretation is supported by mutagenesis studies. When histidine64 is replaced with apolar amino acids, the rate of nitric oxide dissociation from myoglobin increases tenfold. | ||
==About this Structure== | ==About this Structure== | ||
1JDO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with SO4, HEM and NO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1JDO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NO:'>NO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDO OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Brucker, E | [[Category: Brucker, E A.]] | ||
[[Category: Jr., G | [[Category: Jr., G N.Phillips.]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: NO]] | [[Category: NO]] | ||
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[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:29 2008'' | ||
Revision as of 14:21, 21 February 2008
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SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)
OverviewOverview
The structure of the ferrous nitric oxide form of native sperm whale myoglobin has been determined by X-ray crystallography to 1.7 angstroms resolution. The nitric oxide ligand is bent with respect to the heme plane: the Fe-N-O angle is 112 degrees. This angle is smaller than those observed in model compounds and in lupin leghemoglobin. The exact angle appears to be influenced by the strength of the proximal bond and hydrogen bonding interactions between the distal histidine and the bound ligand. Specifically, the N(epsilon) atom of histidine64 is located 2.8 angstroms away from the nitrogen atom of the bound ligand, implying electrostatic stabilization of the FeNO complex. This interpretation is supported by mutagenesis studies. When histidine64 is replaced with apolar amino acids, the rate of nitric oxide dissociation from myoglobin increases tenfold.
About this StructureAbout this Structure
1JDO is a Single protein structure of sequence from Physeter catodon with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Nitric oxide myoglobin: crystal structure and analysis of ligand geometry., Brucker EA, Olson JS, Ikeda-Saito M, Phillips GN Jr, Proteins. 1998 Mar 1;30(4):352-6. PMID:9533619
Page seeded by OCA on Thu Feb 21 13:21:29 2008