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2bc5

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(New page: 200px<br /><applet load="2bc5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bc5, resolution 2.25&Aring;" /> '''Crystal structure of...)
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[[Image:2bc5.gif|left|200px]]<br /><applet load="2bc5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2bc5, resolution 2.25&Aring;" />
 
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'''Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages'''<br />
 
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==Overview==
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==Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages==
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The four-helix-bundle protein fold can be constructed from a wide variety, of primary amino acid sequences. Proteins with this structure are, excellent candidates for investigations of the relationship between, folding mechanism and topology. The folding of cytochrome b(562), a, four-helix-bundle heme protein, is hampered by heme dissociation. To, overcome this complication, we have engineered a variant of cytochrome, b(562) (cyt c-b(562)) featuring a c-type linkage between the heme and the, polypeptide chain. The replacement of the native cyt b(562) leader, sequence in this protein with that of a c-type cytochrome (cyt c(556)) led, to high yields of fully matured and correctly folded cyt c-b(562). We have, determined the X-ray crystal structure of cyt c-b(562) at 2.25 A and, characterized its physical, chemical, and folding properties. These, measurements reveal that the c-type linkage does not perturb the protein, fold or reduction potential of the heme group. The covalent attachment of, the porphyrin to the polypeptide does, however, produce a substantial, change in protein stability and folding kinetics.
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<StructureSection load='2bc5' size='340' side='right'caption='[[2bc5]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bc5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BC5 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]] 2.25&#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=HEC:HEME+C'>HEC</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=2bc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bc5 OCA], [https://pdbe.org/2bc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bc5 RCSB], [https://www.ebi.ac.uk/pdbsum/2bc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bc5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.
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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/bc/2bc5_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=2bc5 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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The four-helix-bundle protein fold can be constructed from a wide variety of primary amino acid sequences. Proteins with this structure are excellent candidates for investigations of the relationship between folding mechanism and topology. The folding of cytochrome b(562), a four-helix-bundle heme protein, is hampered by heme dissociation. To overcome this complication, we have engineered a variant of cytochrome b(562) (cyt c-b(562)) featuring a c-type linkage between the heme and the polypeptide chain. The replacement of the native cyt b(562) leader sequence in this protein with that of a c-type cytochrome (cyt c(556)) led to high yields of fully matured and correctly folded cyt c-b(562). We have determined the X-ray crystal structure of cyt c-b(562) at 2.25 A and characterized its physical, chemical, and folding properties. These measurements reveal that the c-type linkage does not perturb the protein fold or reduction potential of the heme group. The covalent attachment of the porphyrin to the polypeptide does, however, produce a substantial change in protein stability and folding kinetics.
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==About this Structure==
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Stability and folding kinetics of structurally characterized cytochrome c-b562.,Faraone-Mennella J, Tezcan FA, Gray HB, Winkler JR Biochemistry. 2006 Sep 5;45(35):10504-11. PMID:16939202<ref>PMID:16939202</ref>
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2BC5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BC5 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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Stability and folding kinetics of structurally characterized cytochrome c-b562., Faraone-Mennella J, Tezcan FA, Gray HB, Winkler JR, Biochemistry. 2006 Sep 5;45(35):10504-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16939202 16939202]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 2bc5" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Faraone-Mennella, J.]]
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[[Category: Gray, H.B.]]
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[[Category: Tezcan, F.A.]]
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[[Category: Winkler, J.R.]]
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[[Category: HEM]]
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[[Category: SO4]]
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[[Category: four-helix bundle]]
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[[Category: k59w]]
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[[Category: r98c and y101c mutations]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:42:57 2007''
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==See Also==
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*[[Cytochrome b5 3D structures|Cytochrome b5 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: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Faraone-Mennella J]]
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[[Category: Gray HB]]
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[[Category: Tezcan FA]]
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[[Category: Winkler JR]]

Current revision

Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages

PDB ID 2bc5

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