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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1hro]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopila_globiformis Rhodopila globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRO FirstGlance]. <br>
<table><tr><td colspan='2'>[[1hro]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopila_globiformis Rhodopila globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HRO 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></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]] 2.2&#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=1hro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hro OCA], [https://pdbe.org/1hro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hro RCSB], [https://www.ebi.ac.uk/pdbsum/1hro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hro 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=1hro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hro OCA], [https://pdbe.org/1hro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hro RCSB], [https://www.ebi.ac.uk/pdbsum/1hro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hro ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYC2_RHOGL CYC2_RHOGL]
== 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=1hro 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=1hro ConSurf].
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== Publication Abstract from PubMed ==
Unlike their mitochondrial counterparts, the c-type cytochromes typically isolated from photosynthetic nonsulfur purple bacteria display a wide range of oxidation-reduction potentials. Here we describe the X-ray crystallographic analysis of the cytochrome c2 isolated from Rhodopila globiformis. This particular c-type cytochrome was selected for study because of its anomalously high redox potential of +450 mV. Crystals employed in the investigation belonged to the space group I4(1) with unit cell dimensions of a = b = 79.2 A, c = 75.2 A, and two molecules in the asymmetric unit. The structure was solved by the techniques of multiple isomorphous replacement with two heavy-atom derivatives and electron density modification procedures. Least-squares refinement of the model reduced the R-factor to 18.7% for all measured X-ray data from 30.0 to 2.2 A. The overall structural motif of the protein is composed of five alpha-helices, one type I turn, and six type II turns. As in other cytochromes c, there are two conserved water molecules located in the heme-binding pocket. Overall, the three-dimensional structure of the R. globiformis molecule is more similar to the eukaryotic c-type cytochromes than to other bacterial proteins.
Molecular structure of a high potential cytochrome c2 isolated from Rhodopila globiformis.,Benning MM, Meyer TE, Holden HM Arch Biochem Biophys. 1996 Sep 15;333(2):338-48. PMID:8809072<ref>PMID:8809072</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hro" 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: Rhodopila globiformis]]
[[Category: Rhodopila globiformis]]
[[Category: Benning, M M]]
[[Category: Benning MM]]
[[Category: Holden, H M]]
[[Category: Holden HM]]
[[Category: Meyer, T E]]
[[Category: Meyer TE]]
[[Category: Electron transport]]
[[Category: Heme]]
[[Category: Photosynthesis]]

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