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[[Image:1cxy.gif|left|200px]]
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{{STRUCTURE_1cxy|  PDB=1cxy  |  SCENE=  }}
'''STRUCTURE AND CHARACTERIZATION OF ECTOTHIORHODOSPIRA VACUOLATA CYTOCHROME B558, A PROKARYOTIC HOMOLOGUE OF CYTOCHROME B5'''


==STRUCTURE AND CHARACTERIZATION OF ECTOTHIORHODOSPIRA VACUOLATA CYTOCHROME B558, A PROKARYOTIC HOMOLOGUE OF CYTOCHROME B5==
<StructureSection load='1cxy' size='340' side='right'caption='[[1cxy]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cxy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ectothiorhodospira_shaposhnikovii Ectothiorhodospira shaposhnikovii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CXY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1cxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cxy OCA], [https://pdbe.org/1cxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cxy RCSB], [https://www.ebi.ac.uk/pdbsum/1cxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cxy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYB5_ECTSH CYB5_ECTSH]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cx/1cxy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1cxy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A soluble cytochrome b(558) from the purple phototropic bacterium Ectothiorhodospira vacuolata was completely sequenced by a combination of automated Edman degradation and mass spectrometry. The protein, with a measured mass of 10,094.7 Da, contains 90 residues and binds a single protoheme. Unexpectedly, the sequence shows homology to eukaryotic cytochromes b(5). As no prokaryotic homologue had been reported so far, we developed a protocol for the expression, purification, and crystallization of recombinant cytochrome b(558). The structure was solved by molecular replacement to a resolution of 1.65 A. It shows that cytochrome b(558) is indeed the first bacterial cytochrome b(5) to be characterized and differs from its eukaryotic counterparts by the presence of a disulfide bridge and a four-residue insertion in front of the sixth ligand (histidine). Eukaryotes contain a variety of b(5) homologues, including soluble and membrane-bound multifunctional proteins as well as multidomain enzymes such as sulfite oxidase, fatty-acid desaturase, nitrate reductase, and lactate dehydrogenase. A search of the Mycobacterium tuberculosis genome showed that a previously unidentified gene encodes a fatty-acid desaturase with an N-terminal b(5) domain. Thus, it may provide another example of a bacterial b(5) homologue.


==Overview==
Structure and characterization of Ectothiorhodospira vacuolata cytochrome b(558), a prokaryotic homologue of cytochrome b(5).,Kostanjevecki V, Leys D, Van Driessche G, Meyer TE, Cusanovich MA, Fischer U, Guisez Y, Van Beeumen J J Biol Chem. 1999 Dec 10;274(50):35614-20. PMID:10585439<ref>PMID:10585439</ref>
A soluble cytochrome b(558) from the purple phototropic bacterium Ectothiorhodospira vacuolata was completely sequenced by a combination of automated Edman degradation and mass spectrometry. The protein, with a measured mass of 10,094.7 Da, contains 90 residues and binds a single protoheme. Unexpectedly, the sequence shows homology to eukaryotic cytochromes b(5). As no prokaryotic homologue had been reported so far, we developed a protocol for the expression, purification, and crystallization of recombinant cytochrome b(558). The structure was solved by molecular replacement to a resolution of 1.65 A. It shows that cytochrome b(558) is indeed the first bacterial cytochrome b(5) to be characterized and differs from its eukaryotic counterparts by the presence of a disulfide bridge and a four-residue insertion in front of the sixth ligand (histidine). Eukaryotes contain a variety of b(5) homologues, including soluble and membrane-bound multifunctional proteins as well as multidomain enzymes such as sulfite oxidase, fatty-acid desaturase, nitrate reductase, and lactate dehydrogenase. A search of the Mycobacterium tuberculosis genome showed that a previously unidentified gene encodes a fatty-acid desaturase with an N-terminal b(5) domain. Thus, it may provide another example of a bacterial b(5) homologue.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1CXY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ectothiorhodospira_shaposhnikovii Ectothiorhodospira shaposhnikovii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXY OCA].
</div>
<div class="pdbe-citations 1cxy" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structure and characterization of Ectothiorhodospira vacuolata cytochrome b(558), a prokaryotic homologue of cytochrome b(5)., Kostanjevecki V, Leys D, Van Driessche G, Meyer TE, Cusanovich MA, Fischer U, Guisez Y, Van Beeumen J, J Biol Chem. 1999 Dec 10;274(50):35614-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10585439 10585439]
*[[Cytochrome b5 3D structures|Cytochrome b5 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ectothiorhodospira shaposhnikovii]]
[[Category: Ectothiorhodospira shaposhnikovii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Beeumen, J Van.]]
[[Category: Cusanovich MA]]
[[Category: Cusanovich, M A.]]
[[Category: Fischer U]]
[[Category: Driessche, G Van.]]
[[Category: Guisez Y]]
[[Category: Fischer, U.]]
[[Category: Kostanjevecki V]]
[[Category: Guisez, Y.]]
[[Category: Leys D]]
[[Category: Kostanjevecki, V.]]
[[Category: Meyer TE]]
[[Category: Leys, D.]]
[[Category: Van Beeumen J]]
[[Category: Meyer, T E.]]
[[Category: Van Driessche G]]
[[Category: Beta-strand]]
[[Category: Helix]]
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Retrieved from "https://proteopedia.org/1cxy"