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| [[Image:3hip.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_3hip| PDB=3hip | SCENE= }} | | {{STRUCTURE_3hip| PDB=3hip | SCENE= }} |
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| '''HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM'''
| | ===HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM=== |
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| ==Overview==
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| The crystal structure of the high-potential iron-sulfur protein (HiPIP) isolated from Chromatium purpuratum is reported at 2.7 A resolution. The three HiPIP molecules in the asymmetric unit of the crystals form one and one-half dimers. Two molecules are related by a noncrystallographic symmetry rotation of approximately 175 degrees with negligible translation along the dyad axis. The third molecule in the asymmetric unit also forms a dimer with a second HiPIP molecule across the crystallographic 2-fold symmetry axis. The Fe4S4 clusters in both the crystallographic and noncrystallographic dimers are separated by approximately 13.0 A. Solution studies give mixed results regarding the oligomeric state of the C. purpuratum HiPIP. A comparison with crystal structures of HiPIPs from other species shows that HiPIP tends to associate rather nonspecifically about a conserved, relatively hydrophobic surface patch to form dimers. | | The line below this paragraph, {{ABSTRACT_PUBMED_9760225}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9760225 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9760225}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Metalloprotein]] | | [[Category: Metalloprotein]] |
| [[Category: Photosynthesis]] | | [[Category: Photosynthesis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:03:58 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 12:49:14 2008'' |