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2hip

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{{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'''
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===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.
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{{ABSTRACT_PUBMED_1917989}}
==About this Structure==
==About this Structure==
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[[Category: Meyer, T E.]]
[[Category: Meyer, T E.]]
[[Category: Rayment, I.]]
[[Category: Rayment, I.]]
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Revision as of 21:39, 27 July 2008

Image:2hip.png

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

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