2e2y: Difference between revisions
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'''Crystal Structure of F43W/H64D/V68I Myoglobin''' | {{Structure | ||
|PDB= 2e2y |SIZE=350|CAPTION= <scene name='initialview01'>2e2y</scene>, resolution 1.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of F43W/H64D/V68I Myoglobin''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2E2Y is a [ | 2E2Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E2Y OCA]. | ||
==Reference== | ==Reference== | ||
Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants., Watanabe Y, Nakajima H, Ueno T, Acc Chem Res. 2007 Jul;40(7):554-62. Epub 2007 Jun 14. PMID:[http:// | Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants., Watanabe Y, Nakajima H, Ueno T, Acc Chem Res. 2007 Jul;40(7):554-62. Epub 2007 Jun 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17567089 17567089] | ||
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxygen storage/transport]] | [[Category: oxygen storage/transport]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:34:36 2008'' | ||
Revision as of 14:34, 20 March 2008
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| 2e2y, resolution 1.60Å | |||||||||||||
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| Ligands: | SO4, HEM and GOL | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of F43W/H64D/V68I Myoglobin
Overview
A series of myoglobin mutants, in which distal sites are modified by site-directed mutagenesis, are able to catalyze peroxidase, catalase, and P450 reactions even though their proximal histidine ligands are intact. More importantly, reactions of P450, catalase, and peroxidase substrates and compound I of myoglobin mutants can be observed spectroscopically. Thus, detailed oxidation mechanisms were examined. On the basis of these results, we suggest that the different reactivities of P450, catalase, and peroxidase are mainly caused by their active site structures, but not the axial ligand. We have also prepared compound 0 under physiological conditions by employing a mutant of cytochrome c 552. Compound 0 is not able to oxidize ascorbic acid.
About this Structure
2E2Y is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants., Watanabe Y, Nakajima H, Ueno T, Acc Chem Res. 2007 Jul;40(7):554-62. Epub 2007 Jun 14. PMID:17567089
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