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[[Image:1put.gif|left|200px]]


{{Structure
==AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED PUTIDAREDOXIN, A 2FE, 2-S FERREDOXIN FROM PSEUDOMONAS==
|PDB= 1put |SIZE=350|CAPTION= <scene name='initialview01'>1put</scene>
<StructureSection load='1put' size='340' side='right'caption='[[1put]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene>
<table><tr><td colspan='2'>[[1put]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PUT FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR,  models</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1put FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1put OCA], [https://pdbe.org/1put PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1put RCSB], [https://www.ebi.ac.uk/pdbsum/1put PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1put ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pu/1put_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1put ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED PUTIDAREDOXIN, A 2FE, 2-S FERREDOXIN FROM PSEUDOMONAS'''
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<ref>PMID:8204575</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1put" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1PUT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUT OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/8204575 8204575]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Single protein]]
[[Category: Lyons TA]]
[[Category: Lyons, T A.]]
[[Category: Pochapsky TC]]
[[Category: Pochapsky, T C.]]
[[Category: Ratnaswamy G]]
[[Category: Ratnaswamy, G.]]
[[Category: Ye XM]]
[[Category: Ye, X M.]]
[[Category: FES]]
[[Category: electron transport]]
 
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Retrieved from "https://proteopedia.org/1put"