1jdo: Difference between revisions

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[[Image:1jdo.gif|left|200px]]
[[Image:1jdo.gif|left|200px]]


{{Structure
<!--
|PDB= 1jdo |SIZE=350|CAPTION= <scene name='initialview01'>1jdo</scene>, resolution 1.90&Aring;
The line below this paragraph, containing "STRUCTURE_1jdo", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE=
-->
|DOMAIN=
{{STRUCTURE_1jdo| PDB=1jdo  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdo OCA], [http://www.ebi.ac.uk/pdbsum/1jdo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jdo RCSB]</span>
}}


'''SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)'''
'''SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)'''
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[[Category: Brucker, E A.]]
[[Category: Brucker, E A.]]
[[Category: Jr., G N.Phillips.]]
[[Category: Jr., G N.Phillips.]]
[[Category: globin]]
[[Category: Globin]]
[[Category: heme]]
[[Category: Heme]]
[[Category: nitric oxide]]
[[Category: Nitric oxide]]
[[Category: oxygen storage]]
[[Category: Oxygen storage]]
[[Category: oxygen transport]]
[[Category: Oxygen transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:05:55 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:10 2008''

Revision as of 21:05, 2 May 2008

File:1jdo.gif

Template:STRUCTURE 1jdo

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. 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 Fri May 2 21:05:55 2008

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