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1hro
From Proteopedia
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|PDB= 1hro |SIZE=350|CAPTION= <scene name='initialview01'>1hro</scene>, resolution 2.2Å | |PDB= 1hro |SIZE=350|CAPTION= <scene name='initialview01'>1hro</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hro OCA], [http://www.ebi.ac.uk/pdbsum/1hro PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hro RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Holden, H M.]] | [[Category: Holden, H M.]] | ||
[[Category: Meyer, T E.]] | [[Category: Meyer, T E.]] | ||
| - | [[Category: HEM]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: heme]] | [[Category: heme]] | ||
[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:34 2008'' |
Revision as of 18:09, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MOLECULAR STRUCTURE OF A HIGH POTENTIAL CYTOCHROME C2 ISOLATED FROM RHODOPILA GLOBIFORMIS
Overview
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.
About this Structure
1HRO is a Single protein structure of sequence from Rhodopila globiformis. Full crystallographic information is available from OCA.
Reference
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
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