2evk: Difference between revisions
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[[Image:2evk.gif|left|200px]] | [[Image:2evk.gif|left|200px]] | ||
'''The Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models for Cytochrome P450 and for Oxyanion-Bound Heme Proteins''' | {{Structure | ||
|PDB= 2evk |SIZE=350|CAPTION= <scene name='initialview01'>2evk</scene>, resolution 1.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | |||
|ACTIVITY= | |||
|GENE= MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 Physeter catodon]) | |||
}} | |||
'''The Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models for Cytochrome P450 and for Oxyanion-Bound Heme Proteins''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2EVK is a [ | 2EVK 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=2EVK OCA]. | ||
==Reference== | ==Reference== | ||
Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins., Qin J, Perera R, Lovelace LL, Dawson JH, Lebioda L, Biochemistry. 2006 Mar 14;45(10):3170-7. PMID:[http:// | Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins., Qin J, Perera R, Lovelace LL, Dawson JH, Lebioda L, Biochemistry. 2006 Mar 14;45(10):3170-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16519512 16519512] | ||
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: heme]] | [[Category: heme]] | ||
''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 16:44:54 2008'' | ||
Revision as of 17:44, 20 March 2008
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| , resolution 1.40Å | |||||||
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| Ligands: | and | ||||||
| Gene: | MB (Physeter catodon) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models for Cytochrome P450 and for Oxyanion-Bound Heme Proteins
OverviewOverview
Crystal structures of the ferric H93G myoglobin (Mb) cavity mutant containing either an anionic proximal thiolate sulfur donor or a carboxylate oxygen donor ligand are reported at 1.7 and 1.4 A resolution, respectively. The crystal structure and magnetic circular dichroism spectra of the H93G Mb beta-mercaptoethanol (BME) thiolate adduct reveal a high-spin, five-coordinate complex. Furthermore, the bound BME appears to have an intramolecular hydrogen bond involving the alcohol proton and the ligated thiolate sulfur, mimicking one of the three proximal N-H...S hydrogen bonds in cytochrome P450. The Fe is displaced from the porphyrin plane by 0.5 A and forms a 2.41 A Fe-S bond. The Fe(3+)-S-C angle is 111 degrees , indicative of a covalent Fe-S bond with sp(3)-hybridized sulfur. Therefore, the H93G Mb.BME complex provides an excellent protein-derived structural model for high-spin ferric P450. In particular, the Fe-S bond in high-spin ferric P450-CAM has essentially the same geometry despite the constraints imposed by covalent linkage of the cysteine to the protein backbone. This suggests that evolution led to the geometric optimization of the proximal Fe-S(cysteinate) bond in P450. The crystal structure and spectral properties of the H93G Mb acetate adduct reveal a high-spin, six-coordinate complex with proximal acetate and distal water axial ligands. The distal His-64 forms a hydrogen bond with the bound water. The Fe-acetate bonding geometry is inconsistent with an electron pair along the Fe-O bond as the Fe-O-C angle is 152 degrees and the Fe is far from the plane of the acetate. Thus, the Fe-O bonding is ionic. The H93G Mb cavity mutant has already been shown to be a versatile model system for the study of ligand binding to heme proteins; this investigation affords the first structural evidence that nonimidazole exogenous ligands bind in the proximal ligation site.
About this StructureAbout this Structure
2EVK is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
ReferenceReference
Structures of thiolate- and carboxylate-ligated ferric H93G myoglobin: models for cytochrome P450 and for oxyanion-bound heme proteins., Qin J, Perera R, Lovelace LL, Dawson JH, Lebioda L, Biochemistry. 2006 Mar 14;45(10):3170-7. PMID:16519512
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