1ku5

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(New page: 200px<br /><applet load="1ku5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ku5, resolution 2.3&Aring;" /> '''Crystal Structure of ...)
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'''Crystal Structure of recombinant histone HPhA from hyperthermophilic archaeon Pyrococcus horikoshii OT3'''<br />
'''Crystal Structure of recombinant histone HPhA from hyperthermophilic archaeon Pyrococcus horikoshii OT3'''<br />
==Overview==
==Overview==
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The histone protein HPhA from the hyperthermophilic archaeon Pyrococcus, horikoshii, shows hyperthermostability, as required for optimal growth of, the organism at 95 degrees C. The structure of recombinant P.horikoshii, HPhA has been determined to 2.3A resolution by molecular replacement, and, refined to R(work) and R(free) values of 20.7% and 27.3%, respectively., The HPhA monomer structure is characterized by the histone fold and, assembles into a homodimer like other archaeal histones. There are four, anions found in the dimer structure, giving rise to clues as to where DNA, might bind. A detailed comparison of four known structures of archaeal, histones, which evolve and exist under different temperatures, shows that, the thermophilic archaeal histone HPhA has a larger hydrophobic contact, area, an increased number of hydrogen bonds and a reduced, solvent-accessible area. We also observe a unique network of tyrosine, residues located at the crossover point of the two HPhA monomers, which, locks them together and stabilizes the dimer. These factors together, account for the increased thermal stability.
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The histone protein HPhA from the hyperthermophilic archaeon Pyrococcus horikoshii, shows hyperthermostability, as required for optimal growth of the organism at 95 degrees C. The structure of recombinant P.horikoshii HPhA has been determined to 2.3A resolution by molecular replacement, and refined to R(work) and R(free) values of 20.7% and 27.3%, respectively. The HPhA monomer structure is characterized by the histone fold and assembles into a homodimer like other archaeal histones. There are four anions found in the dimer structure, giving rise to clues as to where DNA might bind. A detailed comparison of four known structures of archaeal histones, which evolve and exist under different temperatures, shows that the thermophilic archaeal histone HPhA has a larger hydrophobic contact area, an increased number of hydrogen bonds and a reduced solvent-accessible area. We also observe a unique network of tyrosine residues located at the crossover point of the two HPhA monomers, which locks them together and stabilizes the dimer. These factors together account for the increased thermal stability.
==About this Structure==
==About this Structure==
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1KU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with ACT and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KU5 OCA].
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1KU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU5 OCA].
==Reference==
==Reference==
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[[Category: histone fold]]
[[Category: histone fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:52:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:00 2008''

Revision as of 11:38, 21 February 2008

Image:1ku5.jpg

1ku5, resolution 2.3Å

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Crystal Structure of recombinant histone HPhA from hyperthermophilic archaeon Pyrococcus horikoshii OT3

Overview

The histone protein HPhA from the hyperthermophilic archaeon Pyrococcus horikoshii, shows hyperthermostability, as required for optimal growth of the organism at 95 degrees C. The structure of recombinant P.horikoshii HPhA has been determined to 2.3A resolution by molecular replacement, and refined to R(work) and R(free) values of 20.7% and 27.3%, respectively. The HPhA monomer structure is characterized by the histone fold and assembles into a homodimer like other archaeal histones. There are four anions found in the dimer structure, giving rise to clues as to where DNA might bind. A detailed comparison of four known structures of archaeal histones, which evolve and exist under different temperatures, shows that the thermophilic archaeal histone HPhA has a larger hydrophobic contact area, an increased number of hydrogen bonds and a reduced solvent-accessible area. We also observe a unique network of tyrosine residues located at the crossover point of the two HPhA monomers, which locks them together and stabilizes the dimer. These factors together account for the increased thermal stability.

About this Structure

1KU5 is a Single protein structure of sequence from Pyrococcus horikoshii with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure based hyperthermostability of archaeal histone HPhA from Pyrococcus horikoshii., Li T, Sun F, Ji X, Feng Y, Rao Z, J Mol Biol. 2003 Jan 31;325(5):1031-7. PMID:12527306

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