From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1yoi.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1yoi.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1yoi| PDB=1yoi | SCENE= }} | | {{STRUCTURE_1yoi| PDB=1yoi | SCENE= }} |
| | | | |
| - | '''COBALT MYOGLOBIN (OXY)'''
| + | ===COBALT MYOGLOBIN (OXY)=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The structures of the deoxy, oxy, and aquomet forms of native sperm whale myoglobin reconstituted with cobalt protoporphyrin IX have been determined by x-ray crystallography. As expected, cobalt myoglobin closely resembles native iron myoglobin in overall structure, especially in their respective aquomet forms. In the cobalt oxymyoglobin structure, the Nepsilon of distal histidine 64 lies within hydrogen bonding distance to both the oxygen atom directly bonded to the cobalt and the terminal oxygen atom, in agreement with previous EPR and resonance Raman studies. The metal atom in cobaltous myoglobin does show a small 0.06-A out-of-porphyrin plane displacement when moving from the oxy to deoxy state. In the case of the native iron-containing myoglobin, the oxy to deoxy transition results in a larger 0.16-A displacement of the metal farther out of the porphyrin plane, attributed to an increase in spin from S = 0 to S = 2. The small displacement in cobalt myoglobin is due to a change in coordination geometry, not spin state (S = 1/2 for both cobalt deoxy- and oxymyoglobin). The small out-of-porphyrin plane movement of cobalt which accompanies deoxygenation of myoglobin also occurs in cobalt hemoglobin and serves to explain why cooperativity, although reduced, is still preserved when iron is replaced by cobalt in human hemoglobin. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8810310}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8810310 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_8810310}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Oxygen transport]] | | [[Category: Oxygen transport]] |
| | [[Category: Respiratory protein]] | | [[Category: Respiratory protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:35:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:16:53 2008'' |
Revision as of 00:16, 29 July 2008
Template:STRUCTURE 1yoi
COBALT MYOGLOBIN (OXY)
Template:ABSTRACT PUBMED 8810310
About this Structure
1YOI is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin., Brucker EA, Olson JS, Phillips GN Jr, Dou Y, Ikeda-Saito M, J Biol Chem. 1996 Oct 11;271(41):25419-22. PMID:8810310
Page seeded by OCA on Tue Jul 29 03:16:53 2008
