2bc5

From Proteopedia

(Difference between revisions)

Revision as of 07:36, 23 August 2023

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

Structural highlights

2bc5 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.25Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C562_ECOLX Electron-transport protein of unknown function.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Faraone-Mennella J, Tezcan FA, Gray HB, Winkler JR. Stability and folding kinetics of structurally characterized cytochrome c-b562. Biochemistry. 2006 Sep 5;45(35):10504-11. PMID:16939202 doi:10.1021/bi060242x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bc5"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bc5' size='340' side='right'caption='[[2bc5]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bc5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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>
+<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>
-</td></tr><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>
+</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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[256b|256b]]</div></td></tr>
+<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>
 <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>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX]] Electron-transport protein of unknown function.
+[https://www.uniprot.org/uniprot/C562_ECOLX C562_ECOLX] Electron-transport protein of unknown function.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Faraone-Mennella, J]]
+[[Category: Faraone-Mennella J]]
-[[Category: Gray, H B]]
+[[Category: Gray HB]]
-[[Category: Tezcan, F A]]
+[[Category: Tezcan FA]]
-[[Category: Winkler, J R]]
+[[Category: Winkler JR]]
-[[Category: Electron transport]]
-[[Category: Four-helix bundle]]
-[[Category: K59w]]
-[[Category: R98c and y101c mutation]]

2bc5

From Proteopedia

Revision as of 07:36, 23 August 2023

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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