2axx: Difference between revisions
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[[Image:2axx.gif|left|200px]]<br /> | [[Image:2axx.gif|left|200px]]<br /><applet load="2axx" size="450" color="white" frame="true" align="right" spinBox="true" | ||
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'''THE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, NMR, 21 STRUCTURES'''<br /> | '''THE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, NMR, 21 STRUCTURES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2AXX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. | 2AXX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=NUL:Heme Site'>NUL</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AXX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:43:48 2007'' | ||
Revision as of 19:34, 18 December 2007
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THE SOLUTION STRUCTURE OF OXIDIZED RAT MICROSOMAL CYTOCHROME B5, NMR, 21 STRUCTURES
OverviewOverview
The solution structure of oxidized rat microsomal cytochrome b5 has been, obtained from 1H NMR spectra measured at 800 MHz. The available assignment, has been extended to 78% of the total protons and 95% of the residues., From 1372 meaningful NOEs, a family of 40 structures has been obtained, through the program DYANA; 235 pseudocontact shifts have been then added, as further constraints, obtaining an essentially similar family of, structures. This latter family has been further refined through restrained, energy minimization. The final RMSD values with respect to the average, structure are 0.58 +/- 0.10 A and 1.05 +/- 0.11 A for backbone and heavy, atoms, respectively. The high quality of the structure allows meaningful, comparisons with the solution structure of the reduced protein, with the, X-ray and solution structures of the oxidized bovine isoenzyme, and with, the solution structure of the apoprotein. Upon loss of one electron, the, heme plane undergoes a change in its orientation, possibly due to the, change of the total charge. Propionate 7 appears to have a conformation, which is dependent on the oxidation state of the iron. Helices alpha2 and, alpha4 also experience changes in their average positions in the two, oxidation states. Finally, the backbone NHs experience different exchange, properties in the two oxidation states. While those present in the beta, sheets forming the basis of the heme pocket are nonexchanging in both, oxidation states, the NHs in the helices forming the heme-binding pocket, are exchanging with the bulk solvent in the oxidized form, indicating, larger local mobility in this state. This observation could suggest that, to optimize the electron transfer process, the local mobility should be, properly tuned.
About this StructureAbout this Structure
2AXX is a Single protein structure of sequence from Rattus norvegicus with HEM as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
The solution structure of oxidized rat microsomal cytochrome b5., Arnesano F, Banci L, Bertini I, Felli IC, Biochemistry. 1998 Jan 6;37(1):173-84. PMID:9425037
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