3hip: Difference between revisions

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New page: left|200px<br /><applet load="3hip" size="450" color="white" frame="true" align="right" spinBox="true" caption="3hip, resolution 2.8Å" /> '''HIGH-POTENTIAL IRON-S...
 
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[[Image:3hip.jpg|left|200px]]<br /><applet load="3hip" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:3hip.jpg|left|200px]]<br /><applet load="3hip" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="3hip, resolution 2.8&Aring;" />
caption="3hip, resolution 2.8&Aring;" />
'''HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM'''<br />
'''HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM'''<br />


==Overview==
==Overview==
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 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 Structure==
==About this Structure==
3HIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Marichromatium_purpuratum Marichromatium purpuratum] with SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3HIP OCA].  
3HIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Marichromatium_purpuratum Marichromatium purpuratum] with <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HIP OCA].  


==Reference==
==Reference==
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[[Category: Marichromatium purpuratum]]
[[Category: Marichromatium purpuratum]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kerfeld, C.A.]]
[[Category: Kerfeld, C A.]]
[[Category: Salmeen, A.E.]]
[[Category: Salmeen, A E.]]
[[Category: Yeates, T.O.]]
[[Category: Yeates, T O.]]
[[Category: SF4]]
[[Category: SF4]]
[[Category: electron transfer]]
[[Category: electron transfer]]
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[[Category: photosynthesis]]
[[Category: photosynthesis]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:09:45 2008''

Revision as of 20:09, 21 February 2008

File:3hip.jpg


3hip, resolution 2.8Å

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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 with as ligand. 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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