2bc5

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[[Image:2bc5.gif|left|200px]]
 
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{{Structure
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==Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages==
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|PDB= 2bc5 |SIZE=350|CAPTION= <scene name='initialview01'>2bc5</scene>, resolution 2.25&Aring;
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<StructureSection load='2bc5' size='340' side='right'caption='[[2bc5]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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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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|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]] 2.25&#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=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=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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|RELATEDENTRY=[[256b|256B]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bc5 OCA], [http://www.ebi.ac.uk/pdbsum/2bc5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bc5 RCSB]</span>
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== Function ==
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}}
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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/initialview03.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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'''Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2bc5" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2BC5 is a [[Single protein]] structure of sequence from [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/16939202 16939202]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Faraone-Mennella, J.]]
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[[Category: Faraone-Mennella J]]
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[[Category: Gray, H B.]]
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[[Category: Gray HB]]
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[[Category: Tezcan, F A.]]
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[[Category: Tezcan FA]]
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[[Category: Winkler, J R.]]
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[[Category: Winkler JR]]
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[[Category: four-helix bundle]]
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[[Category: k59w]]
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[[Category: r98c and y101c mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:04:12 2008''
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Current revision

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

PDB ID 2bc5

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