1wtf

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(New page: 200px<br /><applet load="1wtf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wtf, resolution 1.60&Aring;" /> '''Crystal structure of...)
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[[Image:1wtf.gif|left|200px]]<br /><applet load="1wtf" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wtf, resolution 1.60&Aring;" />
 
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'''Crystal structure of Bacillus thermoproteolyticus Ferredoxin Variants Containing Unexpected [3Fe-4S] Cluster that is linked to Coenzyme A at 1.6 A Resolution'''<br />
 
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==Overview==
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==Crystal structure of Bacillus thermoproteolyticus Ferredoxin Variants Containing Unexpected [3Fe-4S] Cluster that is linked to Coenzyme A at 1.6 A Resolution==
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During the purification of recombinant Bacillus thermoproteolyticus, ferredoxin (BtFd) from Escherichia coli, we have noted that some Fe-S, proteins were produced in relatively small amounts compared to the, originally identified BtFd carrying a [4Fe-4S] cluster. These variants, could be purified into three Fe-S protein components (designated as V-I, V-II, and V-III) by standard chromatography procedures. UV-vis and EPR, spectroscopic analyses indicated that each of these variants accommodates, a [3Fe-4S] cluster. From mass spectrometric and protein sequence analyses, together with native and SDS gel electrophoresis, we established that V-I, and V-II contain the polypeptide of BtFd associated with acyl carrier, protein (ACP) and with coenzyme A (CoA), respectively, and that V-III is a, BtFd dimer linked by a disulfide bond. The crystal structure of the, BtFd-CoA complex (V-II) determined at 1.6 A resolution revealed that each, of the four complexes in the crystallographic asymmetric unit possesses a, [3Fe-4S] cluster that is coordinated by Cys(11), Cys(17), and Cys(61). The, polypeptide chain of each complex is superimposable onto that of the, original [4Fe-4S] BtFd except for the segment containing Cys(14), the, fourth ligand to the [4Fe-4S] cluster of BtFd. In the variant molecules, the side chain of Cys(14) is rotated away to the molecular surface, forming a disulfide bond with the terminal sulfhydryl group of CoA. This, covalent modification may have occurred in vivo, thereby preventing the, assembly of the [4Fe-4S] cluster as observed previously for Desulfovibrio, gigas ferredoxin. Possibilities concerning how the variant molecules are, formed in the cell are discussed.
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<StructureSection load='1wtf' size='340' side='right'caption='[[1wtf]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wtf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WTF FirstGlance]. <br>
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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]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1wtf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wtf OCA], [https://pdbe.org/1wtf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wtf RCSB], [https://www.ebi.ac.uk/pdbsum/1wtf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wtf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FER_BACTH FER_BACTH] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
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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/wt/1wtf_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=1wtf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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During the purification of recombinant Bacillus thermoproteolyticus ferredoxin (BtFd) from Escherichia coli, we have noted that some Fe-S proteins were produced in relatively small amounts compared to the originally identified BtFd carrying a [4Fe-4S] cluster. These variants could be purified into three Fe-S protein components (designated as V-I, V-II, and V-III) by standard chromatography procedures. UV-vis and EPR spectroscopic analyses indicated that each of these variants accommodates a [3Fe-4S] cluster. From mass spectrometric and protein sequence analyses together with native and SDS gel electrophoresis, we established that V-I and V-II contain the polypeptide of BtFd associated with acyl carrier protein (ACP) and with coenzyme A (CoA), respectively, and that V-III is a BtFd dimer linked by a disulfide bond. The crystal structure of the BtFd-CoA complex (V-II) determined at 1.6 A resolution revealed that each of the four complexes in the crystallographic asymmetric unit possesses a [3Fe-4S] cluster that is coordinated by Cys(11), Cys(17), and Cys(61). The polypeptide chain of each complex is superimposable onto that of the original [4Fe-4S] BtFd except for the segment containing Cys(14), the fourth ligand to the [4Fe-4S] cluster of BtFd. In the variant molecules, the side chain of Cys(14) is rotated away to the molecular surface, forming a disulfide bond with the terminal sulfhydryl group of CoA. This covalent modification may have occurred in vivo, thereby preventing the assembly of the [4Fe-4S] cluster as observed previously for Desulfovibrio gigas ferredoxin. Possibilities concerning how the variant molecules are formed in the cell are discussed.
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==About this Structure==
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Identification of variant molecules of Bacillus thermoproteolyticus ferredoxin: crystal structure reveals bound coenzyme A and an unexpected [3Fe-4S] cluster associated with a canonical [4Fe-4S] ligand motif.,Shirakawa T, Takahashi Y, Wada K, Hirota J, Takao T, Ohmori D, Fukuyama K Biochemistry. 2005 Sep 20;44(37):12402-10. PMID:16156653<ref>PMID:16156653</ref>
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1WTF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus] with SO4, COA and F3S as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WTF OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Identification of variant molecules of Bacillus thermoproteolyticus ferredoxin: crystal structure reveals bound coenzyme A and an unexpected [3Fe-4S] cluster associated with a canonical [4Fe-4S] ligand motif., Shirakawa T, Takahashi Y, Wada K, Hirota J, Takao T, Ohmori D, Fukuyama K, Biochemistry. 2005 Sep 20;44(37):12402-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16156653 16156653]
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</div>
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[[Category: Bacillus thermoproteolyticus]]
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<div class="pdbe-citations 1wtf" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Fukuyama, K.]]
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[[Category: Hirota, J.]]
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[[Category: Ohmori, D.]]
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[[Category: Shirakawa, T.]]
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[[Category: Takahashi, Y.]]
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[[Category: Takao, T.]]
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[[Category: Wada, K.]]
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[[Category: COA]]
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[[Category: F3S]]
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[[Category: SO4]]
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[[Category: 3fe-4s cluster]]
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[[Category: coenzyme a]]
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[[Category: complex]]
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[[Category: ferredoxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:39:35 2007''
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==See Also==
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*[[Ferredoxin 3D structures|Ferredoxin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus thermoproteolyticus]]
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[[Category: Large Structures]]
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[[Category: Fukuyama K]]
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[[Category: Hirota J]]
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[[Category: Ohmori D]]
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[[Category: Shirakawa T]]
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[[Category: Takahashi Y]]
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[[Category: Takao T]]
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[[Category: Wada K]]

Current revision

Crystal structure of Bacillus thermoproteolyticus Ferredoxin Variants Containing Unexpected [3Fe-4S] Cluster that is linked to Coenzyme A at 1.6 A Resolution

PDB ID 1wtf

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