1hlq

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(New page: 200px<br /><applet load="1hlq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hlq, resolution 1.45&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hlq.jpg|left|200px]]<br /><applet load="1hlq" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hlq.jpg|left|200px]]<br /><applet load="1hlq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hlq, resolution 1.45&Aring;" />
caption="1hlq, resolution 1.45&Aring;" />
'''CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A'''<br />
'''CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A'''<br />
==Overview==
==Overview==
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The crystal structure of Rhodoferax fermentans high-potential iron protein, (HiPIP) has been solved by MAD methods using the anomalous signal from the, Fe atoms in the [Fe(4)S(4)] cluster present in the protein and refined to, a resolution of 1.45 A. The peptide chain is well defined except in the N-, and C-terminal areas. The structure of the protein reveals the presence of, three helical fragments, a small beta-sheet and several turns, with the, [Fe(4)S(4)] cluster being located close to a surface patch containing, several well conserved aromatic residues. The protein fold is very similar, to the structures of other known HiPIPs, especially in the region proximal, to the [Fe(4)S(4)] cluster, while the largest differences are observed on, the opposite side of the protein, which is rich in positive charges and, has no sequential homology to other HiPIP families.
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The crystal structure of Rhodoferax fermentans high-potential iron protein (HiPIP) has been solved by MAD methods using the anomalous signal from the Fe atoms in the [Fe(4)S(4)] cluster present in the protein and refined to a resolution of 1.45 A. The peptide chain is well defined except in the N- and C-terminal areas. The structure of the protein reveals the presence of three helical fragments, a small beta-sheet and several turns, with the [Fe(4)S(4)] cluster being located close to a surface patch containing several well conserved aromatic residues. The protein fold is very similar to the structures of other known HiPIPs, especially in the region proximal to the [Fe(4)S(4)] cluster, while the largest differences are observed on the opposite side of the protein, which is rich in positive charges and has no sequential homology to other HiPIP families.
==About this Structure==
==About this Structure==
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1HLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodoferax_fermentans Rhodoferax fermentans] with SO4 and SF4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HLQ OCA].
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1HLQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodoferax_fermentans Rhodoferax fermentans] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLQ OCA].
==Reference==
==Reference==
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[[Category: iron sulfur cluster]]
[[Category: iron sulfur cluster]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:38:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:32 2008''

Revision as of 11:02, 21 February 2008


1hlq, resolution 1.45Å

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CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A

Overview

The crystal structure of Rhodoferax fermentans high-potential iron protein (HiPIP) has been solved by MAD methods using the anomalous signal from the Fe atoms in the [Fe(4)S(4)] cluster present in the protein and refined to a resolution of 1.45 A. The peptide chain is well defined except in the N- and C-terminal areas. The structure of the protein reveals the presence of three helical fragments, a small beta-sheet and several turns, with the [Fe(4)S(4)] cluster being located close to a surface patch containing several well conserved aromatic residues. The protein fold is very similar to the structures of other known HiPIPs, especially in the region proximal to the [Fe(4)S(4)] cluster, while the largest differences are observed on the opposite side of the protein, which is rich in positive charges and has no sequential homology to other HiPIP families.

About this Structure

1HLQ is a Single protein structure of sequence from Rhodoferax fermentans with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD., Gonzalez A, Benini S, Ciurli S, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1582-8. Epub 2003, Aug 19. PMID:12925788

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