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[[Image:1nbb.gif|left|200px]]<br /><applet load="1nbb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nbb, resolution 2.4&Aring;" />
'''N-BUTYLISOCYANIDE BOUND RHODOBACTER CAPSULATUS CYTOCHROME C''''<br />


==Overview==
==N-BUTYLISOCYANIDE BOUND RHODOBACTER CAPSULATUS CYTOCHROME C'==
<StructureSection load='1nbb' size='340' side='right'caption='[[1nbb]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nbb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBB 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]] 2.4&#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>, <scene name='pdbligand=NBN:N-BUTYL+ISOCYANIDE'>NBN</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=1nbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbb OCA], [https://pdbe.org/1nbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbb RCSB], [https://www.ebi.ac.uk/pdbsum/1nbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYCP_RHOCA CYCP_RHOCA] Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
== 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/nb/1nbb_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=1nbb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus cytochrome c'. This is the first example of a ligand-bound structure of a class IIa cytochrome c. Compared with the structure of native cytochrome c', there are significant conformational changes of amino acid residues in the haem vicinity, accompanied by a rearrangement of the hydrogen bonding pattern. The results suggest that rearrangements resulting from ligand binding could drive dimer dissociation in some species and also that the haem propionate may participate in proton transfer.
We have determined the structure of n-butylisocyanide-bound Rhodobacter capsulatus cytochrome c'. This is the first example of a ligand-bound structure of a class IIa cytochrome c. Compared with the structure of native cytochrome c', there are significant conformational changes of amino acid residues in the haem vicinity, accompanied by a rearrangement of the hydrogen bonding pattern. The results suggest that rearrangements resulting from ligand binding could drive dimer dissociation in some species and also that the haem propionate may participate in proton transfer.


==About this Structure==
Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c' from rhodobacter capsulatus.,Tahirov TH, Misaki S, Meyer TE, Cusanovich MA, Higuchi Y, Yasuoka N Nat Struct Biol. 1996 May;3(5):459-64. PMID:8612077<ref>PMID:8612077</ref>
1NBB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NBN:'>NBN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBB OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c' from rhodobacter capsulatus., Tahirov TH, Misaki S, Meyer TE, Cusanovich MA, Higuchi Y, Yasuoka N, Nat Struct Biol. 1996 May;3(5):459-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8612077 8612077]
</div>
<div class="pdbe-citations 1nbb" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodobacter capsulatus]]
[[Category: Rhodobacter capsulatus]]
[[Category: Single protein]]
[[Category: Cusanovich MA]]
[[Category: Cusanovich, M A.]]
[[Category: Higuchi Y]]
[[Category: Higuchi, Y.]]
[[Category: Meyer TE]]
[[Category: Meyer, T E.]]
[[Category: Misaki S]]
[[Category: Misaki, S.]]
[[Category: Tahirov TH]]
[[Category: Tahirov, T H.]]
[[Category: Yasuoka N]]
[[Category: Yasuoka, N.]]
[[Category: HEM]]
[[Category: NBN]]
[[Category: cytochrome]]
[[Category: electron transport]]
[[Category: heme protein]]
 
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