1put: Difference between revisions
New page: left|200px<br /><applet load="1put" size="450" color="white" frame="true" align="right" spinBox="true" caption="1put" /> '''AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCT... |
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'''AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED PUTIDAREDOXIN, A 2FE, 2-S FERREDOXIN FROM PSEUDOMONAS'''<br /> | '''AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED PUTIDAREDOXIN, A 2FE, 2-S FERREDOXIN FROM PSEUDOMONAS'''<br /> | ||
==Overview== | ==Overview== | ||
A model for the solution structure of oxidized putidaredoxin (Pdx), a | A model for the solution structure of oxidized putidaredoxin (Pdx), a 106-residue globular protein containing a Fe2S2 cluster, has been determined using homonuclear NMR methods. Pdx is the first of the class of Fe2S2Cys4 ferredoxins which act as electron-transfer partners for P-450 monooxygenases to be structurally characterized, and no crystal structure has been determined for Pdx or for any closely homologous protein. Pdx is the physiological redox partner of cytochrome P-450cam. A total of 878 NOE distance constraints, 66 phi angular constraints derived from NH-C alpha H coupling constants, and five paramagnetic broadening constraints were used in simulated annealing structural refinements to obtain a family of structures with pairwise rms deviations of 1.14 A for backbone atoms and 1.80 A for all non-hydrogen atoms. Paramagnetic broadening of resonances within a ca. 8-A radius of the metal cluster prevents the use of NMR-derived constraints in this region of the protein; structural constraints used to model the environment of the metal cluster were obtained from site-directed mutagenesis and model compounds and by comparison with known ferredoxin structures. Pdx retains a similar folding topology to other structurally characterized Fe2S2Cys4 ferredoxins but differs from the other ferredoxins in containing a significantly more compact structure in the C-terminal half of the protein. | ||
==About this Structure== | ==About this Structure== | ||
1PUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with FES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1PUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lyons, T | [[Category: Lyons, T A.]] | ||
[[Category: Pochapsky, T | [[Category: Pochapsky, T C.]] | ||
[[Category: Ratnaswamy, G.]] | [[Category: Ratnaswamy, G.]] | ||
[[Category: Ye, X | [[Category: Ye, X M.]] | ||
[[Category: FES]] | [[Category: FES]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:46 2008'' | ||
Revision as of 12:32, 21 February 2008
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AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED PUTIDAREDOXIN, A 2FE, 2-S FERREDOXIN FROM PSEUDOMONAS
Overview
A model for the solution structure of oxidized putidaredoxin (Pdx), a 106-residue globular protein containing a Fe2S2 cluster, has been determined using homonuclear NMR methods. Pdx is the first of the class of Fe2S2Cys4 ferredoxins which act as electron-transfer partners for P-450 monooxygenases to be structurally characterized, and no crystal structure has been determined for Pdx or for any closely homologous protein. Pdx is the physiological redox partner of cytochrome P-450cam. A total of 878 NOE distance constraints, 66 phi angular constraints derived from NH-C alpha H coupling constants, and five paramagnetic broadening constraints were used in simulated annealing structural refinements to obtain a family of structures with pairwise rms deviations of 1.14 A for backbone atoms and 1.80 A for all non-hydrogen atoms. Paramagnetic broadening of resonances within a ca. 8-A radius of the metal cluster prevents the use of NMR-derived constraints in this region of the protein; structural constraints used to model the environment of the metal cluster were obtained from site-directed mutagenesis and model compounds and by comparison with known ferredoxin structures. Pdx retains a similar folding topology to other structurally characterized Fe2S2Cys4 ferredoxins but differs from the other ferredoxins in containing a significantly more compact structure in the C-terminal half of the protein.
About this Structure
1PUT is a Single protein structure of sequence from Pseudomonas putida with FES as ligand. Full crystallographic information is available from OCA.
Reference
An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas., Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA, Biochemistry. 1994 May 31;33(21):6424-32. PMID:8204575
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