3hip: Difference between revisions
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[[Image:3hip.jpg|left|200px]] | [[Image:3hip.jpg|left|200px]] | ||
'''HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM''' | {{Structure | ||
|PDB= 3hip |SIZE=350|CAPTION= <scene name='initialview01'>3hip</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR CLUSTER'>SF4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3HIP is a [ | 3HIP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Marichromatium_purpuratum Marichromatium purpuratum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HIP OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9760225 9760225] | ||
[[Category: Marichromatium purpuratum]] | [[Category: Marichromatium purpuratum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:05:15 2008'' |
Revision as of 20:05, 20 March 2008
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, resolution 2.8Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM
OverviewOverview
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.
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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