1t9p

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[[Image:1t9p.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of V44A, G45P Cp Rubredoxin==
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|PDB= 1t9p |SIZE=350|CAPTION= <scene name='initialview01'>1t9p</scene>, resolution 1.50&Aring;
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<StructureSection load='1t9p' size='340' side='right'caption='[[1t9p]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>
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<table><tr><td colspan='2'>[[1t9p]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T9P FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t9p OCA], [https://pdbe.org/1t9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t9p RCSB], [https://www.ebi.ac.uk/pdbsum/1t9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t9p ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1t9o|1T9O]], [[1t9q|1T9Q]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t9p OCA], [http://www.ebi.ac.uk/pdbsum/1t9p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t9p RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/RUBR_CLOPA RUBR_CLOPA] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t9/1t9p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1t9p ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of V44A, G45P Cp Rubredoxin'''
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==See Also==
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*[[Rubredoxin 3D structures|Rubredoxin 3D structures]]
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*[[Rubredoxin PDB structures|Rubredoxin PDB structures]]
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==Overview==
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__TOC__
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Understanding the structural origins of differences in reduction potentials is crucial to understanding how various electron transfer proteins modulate their reduction potentials and how they evolve for diverse functional roles. Here, the high-resolution structures of several Clostridium pasteurianum rubredoxin (Cp Rd) variants with changes in the vicinity of the redox site are reported in order to increase this understanding. Our crystal structures of [V44L] (at 1.8 A resolution), [V44A] (1.6 A), [V44G] (2.0 A) and [V44A, G45P] (1.5 A) Rd (all in their oxidized states) show that there is a gradual decrease in the distance between Fe and the amide nitrogen of residue 44 upon reduction in the size of the side chain of residue 44; the decrease occurs from leucine to valine, alanine or glycine and is accompanied by a gradual increase in their reduction potentials. Mutation of Cp Rd at position 44 also changes the hydrogen-bond distance between the amide nitrogen of residue 44 and the sulfur of cysteine 42 in a size-dependent manner. Our results suggest that residue 44 is an important determinant of Rd reduction potential in a manner dictated by side-chain size. Along with the electric dipole moment of the 43-44 peptide bond and the 44-42 NH--S type hydrogen bond, a modulation mechanism for solvent accessibility through residue 41 might regulate the redox reaction of the Rds.
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</StructureSection>
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==About this Structure==
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1T9P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T9P OCA].
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==Reference==
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Crystallographic studies of V44 mutants of Clostridium pasteurianum rubredoxin: effects of side-chain size on reduction potential., Park IY, Eidsness MK, Lin IJ, Gebel EB, Youn B, Harley JL, Machonkin TE, Frederick RO, Markley JL, Smith ET, Ichiye T, Kang C, Proteins. 2004 Nov 15;57(3):618-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15382226 15382226]
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[[Category: Clostridium pasteurianum]]
[[Category: Clostridium pasteurianum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Eidsness, M K.]]
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[[Category: Eidsness MK]]
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[[Category: Frederick, R O.]]
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[[Category: Frederick RO]]
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[[Category: Gebel, E B.]]
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[[Category: Gebel EB]]
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[[Category: Harley, J L.]]
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[[Category: Harley JL]]
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[[Category: Ichiye, T.]]
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[[Category: Ichiye T]]
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[[Category: Kang, C.]]
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[[Category: Kang C]]
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[[Category: Lin, I J.]]
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[[Category: Lin IJ]]
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[[Category: Machonkin, T E.]]
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[[Category: Machonkin TE]]
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[[Category: Markley, J L.]]
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[[Category: Markley JL]]
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[[Category: Park, I Y.]]
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[[Category: Park IY]]
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[[Category: Smith, E T.]]
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[[Category: Smith ET]]
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[[Category: Youn, B.]]
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[[Category: Youn B]]
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[[Category: rubredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:16 2008''
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Current revision

Crystal Structure of V44A, G45P Cp Rubredoxin

PDB ID 1t9p

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