1h98
From Proteopedia
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|PDB= 1h98 |SIZE=350|CAPTION= <scene name='initialview01'>1h98</scene>, resolution 1.64Å | |PDB= 1h98 |SIZE=350|CAPTION= <scene name='initialview01'>1h98</scene>, resolution 1.64Å | ||
|SITE= <scene name='pdbsite=FS4:CYS+Residues+8,+16+And+49+Coordinate+The+Fs3'>FS4</scene> | |SITE= <scene name='pdbsite=FS4:CYS+Residues+8,+16+And+49+Coordinate+The+Fs3'>FS4</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h98 OCA], [http://www.ebi.ac.uk/pdbsum/1h98 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h98 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pereira, P J.B.]] | [[Category: Pereira, P J.B.]] | ||
[[Category: Soulimane, T.]] | [[Category: Soulimane, T.]] | ||
| - | [[Category: F3S]] | ||
| - | [[Category: SF4]] | ||
[[Category: azotobacter]] | [[Category: azotobacter]] | ||
[[Category: high resolution]] | [[Category: high resolution]] | ||
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[[Category: thermophilic]] | [[Category: thermophilic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:00:23 2008'' |
Revision as of 18:00, 30 March 2008
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| , resolution 1.64Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NEW INSIGHTS INTO THERMOSTABILITY OF BACTERIAL FERREDOXINS: HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SEVEN-IRON FERREDOXIN FROM THERMUS THERMOPHILUS
Overview
The crystal structure of the seven-iron ferredoxin from Thermus thermophilus (FdTt) has been determined at 1.64 A resolution, allowing us to unveil the common mechanisms of thermostabilization within "bacterial-type" ferredoxins. FdTt and other homologous thermophilic seven-iron ferredoxins are smaller than their mesophilic counterparts. Thermostabilizing features are optimized in a minimal structural and functional unit, with an extensive cross-linking of secondary structure elements mediated by improved polar and hydrophobic interactions. Most of the potentially stabilizing features are focused on the vicinity of the functional [3Fe-4S] cluster. The structural [4Fe-4S] cluster is shielded in thermophilic FdTt by an increased number of polar interactions involving the two N-terminal residues. Comparisons with the hyperthermostable ferredoxin from Thermotoga maritima reveal that (1) a reduction in the number of non-glycine residues in strained conformations, (2) improved polar interactions within the common iron-sulfur cluster binding (betaalphabeta)2 motif, and (3) an optimized charge distribution at the protein surface, constitute a common strategy for increasing the thermal stability of these ferredoxins.
About this Structure
1H98 is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.
Reference
New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus., Macedo-Ribeiro S, Martins BM, Pereira PJ, Buse G, Huber R, Soulimane T, J Biol Inorg Chem. 2001 Sep;6(7):663-74. PMID:11681700
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