1a2s
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Cytochrome c6 from Monoraphidium braunii, an 89-amino acid electron | + | Cytochrome c6 from Monoraphidium braunii, an 89-amino acid electron transfer protein, has been investigated by NMR in solution, in its oxidized form, at pH 7 and 300 K. By using a combination of COSY, TOCSY, and NOESY experiments, 84% of the proton resonances have been assigned. A total of 1668 experimental NOE constraints, 1109 of which were meaningful, together with 288 pseudocontact shifts, have been used to determine the structure in solution. This is represented as a family of 40 structures which have been energy minimized. The rmsd values with respect to the mean structure are 0.57 +/- 0.08 and 0.94 +/- 0.09 A for the backbone and heavy atoms, respectively. The structure has been found to be very similar to that of the reduced form, except for a rearrangement in propionate 7, a feature which has been observed in all c-type cytochromes investigated so far. Such a feature could be relevant for the efficiency of the electron transfer pathway with either the oxidizing or the reducing partners. Other differences in the oxidation states have been noted in the region proposed to be involved in the interaction with the physiological partners. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Bertini, I.]] | [[Category: Bertini, I.]] | ||
[[Category: Koulougliotis, D.]] | [[Category: Koulougliotis, D.]] | ||
| - | [[Category: Navarro, J | + | [[Category: Navarro, J A.]] |
| - | [[Category: Rosa, M | + | [[Category: Rosa, M A.De La.]] |
[[Category: Walter, O.]] | [[Category: Walter, O.]] | ||
[[Category: HEC]] | [[Category: HEC]] | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:15 2008'' |
Revision as of 09:40, 21 February 2008
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THE SOLUTION NMR STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGA MONORAPHIDIUM BRAUNII, MINIMIZED AVERAGE STRUCTURE
Overview
Cytochrome c6 from Monoraphidium braunii, an 89-amino acid electron transfer protein, has been investigated by NMR in solution, in its oxidized form, at pH 7 and 300 K. By using a combination of COSY, TOCSY, and NOESY experiments, 84% of the proton resonances have been assigned. A total of 1668 experimental NOE constraints, 1109 of which were meaningful, together with 288 pseudocontact shifts, have been used to determine the structure in solution. This is represented as a family of 40 structures which have been energy minimized. The rmsd values with respect to the mean structure are 0.57 +/- 0.08 and 0.94 +/- 0.09 A for the backbone and heavy atoms, respectively. The structure has been found to be very similar to that of the reduced form, except for a rearrangement in propionate 7, a feature which has been observed in all c-type cytochromes investigated so far. Such a feature could be relevant for the efficiency of the electron transfer pathway with either the oxidizing or the reducing partners. Other differences in the oxidation states have been noted in the region proposed to be involved in the interaction with the physiological partners.
About this Structure
1A2S is a Single protein structure of sequence from Monoraphidium braunii with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Solution structure of oxidized cytochrome c6 from the green alga Monoraphidium braunii., Banci L, Bertini I, De la Rosa MA, Koulougliotis D, Navarro JA, Walter O, Biochemistry. 1998 Apr 7;37(14):4831-43. PMID:9538000
Page seeded by OCA on Thu Feb 21 11:40:15 2008
