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| | {{STRUCTURE_2hip| PDB=2hip | SCENE= }} | | {{STRUCTURE_2hip| PDB=2hip | SCENE= }} |
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| - | '''THE MOLECULAR STRUCTURE OF THE HIGH POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA HALOPHILA DETERMINED AT 2.5-ANGSTROMS RESOLUTION'''
| + | ===THE MOLECULAR STRUCTURE OF THE HIGH POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA HALOPHILA DETERMINED AT 2.5-ANGSTROMS RESOLUTION=== |
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| - | ==Overview==
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| - | The molecular structure of a high potential iron-sulfur protein (HiPIP) isolated from the purple photosynthetic bacterium, Ectothiorhodospira halophila strain BN9626, has been solved by x-ray diffraction analysis to a nominal resolution of 2.5 A and refined to a crystallographic R value of 18.4% including all measured x-ray data from 30.0- to 2.5-A resolution. Crystals used in the investigation contained two molecules/asymmetric unit and belonged to the space group P21 with unit cell dimensions of a = 60.00 A, b = 31.94 A, c = 40.27 A, and beta = 100.5 degrees. An interpretable electron density map, obtained by combining x-ray data from one isomorphous heavy atom derivative with non-crystallographic symmetry averaging and solvent flattening, clearly showed that this high potential iron-sulfur protein contains 71 amino acid residues, rather than 70 as originally reported. As in other bacterial ferredoxins, the [4Fe-4S] cluster adopts a cubane-like conformation and is ligated to the protein via four cysteinyl sulfur ligands. The overall secondary structure of the E. halophila HiPIP is characterized by a series of Type I and Type II turns allowing the polypeptide chain to wrap around the [4Fe-4S] prosthetic group. The hydrogen bonding pattern around the cluster is nearly identical to that originally observed in the 85-amino acid residue Chromatium vinosum HiPIP and consequently, the 240 mV difference in redox potentials between these two proteins cannot be simply attributed to hydrogen bonding patterns alone. | + | The line below this paragraph, {{ABSTRACT_PUBMED_1917989}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 1917989 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_1917989}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Meyer, T E.]] | | [[Category: Meyer, T E.]] |
| | [[Category: Rayment, I.]] | | [[Category: Rayment, I.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:20:35 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:39:10 2008'' |
Revision as of 21:39, 27 July 2008
Template:STRUCTURE 2hip
THE MOLECULAR STRUCTURE OF THE HIGH POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA HALOPHILA DETERMINED AT 2.5-ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 1917989
About this Structure
2HIP is a Single protein structure of sequence from Halorhodospira halophila. Full crystallographic information is available from OCA.
Reference
The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution., Breiter DR, Meyer TE, Rayment I, Holden HM, J Biol Chem. 1991 Oct 5;266(28):18660-7. PMID:1917989
Page seeded by OCA on Mon Jul 28 00:39:10 2008
