1h98

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[[Image:1h98.gif|left|200px]]<br /><applet load="1h98" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h98.gif|left|200px]]
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caption="1h98, resolution 1.64&Aring;" />
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'''NEW INSIGHTS INTO THERMOSTABILITY OF BACTERIAL FERREDOXINS: HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SEVEN-IRON FERREDOXIN FROM THERMUS THERMOPHILUS'''<br />
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{{Structure
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|PDB= 1h98 |SIZE=350|CAPTION= <scene name='initialview01'>1h98</scene>, resolution 1.64&Aring;
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|SITE= <scene name='pdbsite=FS4:CYS+Residues+8,+16+And+49+Coordinate+The+Fs3'>FS4</scene>
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|LIGAND= <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=F3S:FE3-S4 CLUSTER'>F3S</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''NEW INSIGHTS INTO THERMOSTABILITY OF BACTERIAL FERREDOXINS: HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SEVEN-IRON FERREDOXIN FROM THERMUS THERMOPHILUS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1H98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=F3S:'>F3S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=FS4:CYS+Residues+8,+16+And+49+Coordinate+The+Fs3'>FS4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H98 OCA].
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1H98 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H98 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11681700 11681700]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11681700 11681700]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
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[[Category: azotobacter]]
[[Category: azotobacter]]
[[Category: high resolution]]
[[Category: high resolution]]
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[[Category: hydrogen bonds]]
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[[Category: hydrogen bond]]
[[Category: iron-sulfur]]
[[Category: iron-sulfur]]
[[Category: stability]]
[[Category: stability]]
[[Category: thermophilic]]
[[Category: thermophilic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:34:00 2008''

Revision as of 09:34, 20 March 2008


PDB ID 1h98

Drag the structure with the mouse to rotate
, resolution 1.64Å
Sites:
Ligands: and
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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