3hip: Difference between revisions
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<StructureSection load='3hip' size='340' side='right'caption='[[3hip]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3hip' size='340' side='right'caption='[[3hip]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3hip]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3hip]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HIP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hip OCA], [https://pdbe.org/3hip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hip RCSB], [https://www.ebi.ac.uk/pdbsum/3hip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hip ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HIP_MARPU HIP_MARPU] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Marichromatium purpuratum]] | [[Category: Marichromatium purpuratum]] | ||
[[Category: Kerfeld | [[Category: Kerfeld CA]] | ||
[[Category: Salmeen | [[Category: Salmeen AE]] | ||
[[Category: Yeates | [[Category: Yeates TO]] | ||
Latest revision as of 09:48, 9 August 2023
HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUMHIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM
Structural highlights
FunctionHIP_MARPU Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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