1nbb: Difference between revisions

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== Structural highlights ==
== 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>
<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='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>
</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>
<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>
</table>
== Function ==
== 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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1nbb ConSurf].
</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="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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1nbb" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rhodobacter capsulatus]]
[[Category: Rhodobacter capsulatus]]
[[Category: Cusanovich, M A]]
[[Category: Cusanovich MA]]
[[Category: Higuchi, Y]]
[[Category: Higuchi Y]]
[[Category: Meyer, T E]]
[[Category: Meyer TE]]
[[Category: Misaki, S]]
[[Category: Misaki S]]
[[Category: Tahirov, T H]]
[[Category: Tahirov TH]]
[[Category: Yasuoka, N]]
[[Category: Yasuoka N]]
[[Category: Cytochrome]]
[[Category: Electron transport]]
[[Category: Heme protein]]

Revision as of 11:47, 10 April 2024

N-BUTYLISOCYANIDE BOUND RHODOBACTER CAPSULATUS CYTOCHROME C'N-BUTYLISOCYANIDE BOUND RHODOBACTER CAPSULATUS CYTOCHROME C'

Structural highlights

1nbb is a 2 chain structure with sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

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

See Also

1nbb, resolution 2.40Å

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