2ekt: Difference between revisions
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|PDB= 2ekt |SIZE=350|CAPTION= <scene name='initialview01'>2ekt</scene>, resolution 1.10Å | |PDB= 2ekt |SIZE=350|CAPTION= <scene name='initialview01'>2ekt</scene>, resolution 1.10Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=6HE:6-METHY-6-DEPROPIONATEHEMIN'>6HE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2eku|2EKU]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ekt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ekt OCA], [http://www.ebi.ac.uk/pdbsum/2ekt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ekt RCSB]</span> | |||
}} | }} | ||
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[[Category: Shiro, Y.]] | [[Category: Shiro, Y.]] | ||
[[Category: Sugimoto, H.]] | [[Category: Sugimoto, H.]] | ||
[[Category: globin fold]] | [[Category: globin fold]] | ||
[[Category: oxygen storage/transport complex]] | [[Category: oxygen storage/transport complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:50:34 2008'' | ||
Revision as of 02:50, 31 March 2008
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| , resolution 1.10Å | |||||||
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| Ligands: | , | ||||||
| Related: | 2EKU
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of myoglobin reconstituted with 6-methyl-6-depropionatehemin
OverviewOverview
Two heme propionate side chains, which are attached at the 6 and 7 positions of the heme framework, are linked with Arg45 and Ser92, respectively, in sperm whale myoglobin. To evaluate the role of each propionate, two kinds of one-legged hemins, 6-depropionated and 7-depropionated protohemins, were prepared and inserted into the apomyoglobin to yield two reconstituted proteins. Structural data of the reconstituted myoglobins were obtained via an X-ray crystallographic analysis at a resolution of 1.1-1.4 A and resonance Raman spectroscopy. It was found that the lack of the 6-propionate reduces the number of hydrogen bonds in the distal site and clearly changes the position of the Arg45 residue with the disrupting Arg45-Asp60 interaction. In contrast, the removal of the 7-propionate does not cause a significant structural change in the residues of the distal and proximal sites. However, the resonance Raman studies suggested that the coordination bond strength of the His93-Fe bond for the protein with the 7-depropionated protoheme slightly increases compared to that for the protein with the native heme. The O2 and CO ligand binding studies for the reconstituted proteins with the one-legged hemes provide an important insight into the functional role of each propionate. The lack of the 6-propionate accelerates the O2 dissociation by ca. 3-fold compared to those of the other reconstituted and native proteins. The lack of the 7-propionate enhances the CO affinity by 2-fold compared to that of the protein with the native heme. These results indicate that the 6-propionate clearly contributes to the stabilization of the bound O2, whereas the 7-propionate plays an important role in the regulation of the Fe-His bond.
About this StructureAbout this Structure
2EKT is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
ReferenceReference
Structure and ligand binding properties of myoglobins reconstituted with monodepropionated heme: functional role of each heme propionate side chain., Harada K, Makino M, Sugimoto H, Hirota S, Matsuo T, Shiro Y, Hisaeda Y, Hayashi T, Biochemistry. 2007 Aug 21;46(33):9406-16. Epub 2007 Jul 18. PMID:17636874
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