3hip: Difference between revisions

Revision as of 12:49, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3hip.png

Template:STRUCTURE 3hip

HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUMHIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM

Template:ABSTRACT PUBMED 9760225

About this StructureAbout this Structure

3HIP is a Single protein structure of sequence from Marichromatium purpuratum. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure and possible dimerization of the high-potential iron-sulfur protein from Chromatium purpuratum., Kerfeld CA, Salmeen AE, Yeates TO, Biochemistry. 1998 Oct 6;37(40):13911-7. PMID:9760225

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OCA

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+===HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM===
-==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.
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