1k26
From Proteopedia
(New page: 200px<br /><applet load="1k26" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k26, resolution 1.85Å" /> '''Structure of a Nudix...) |
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| - | [[Image:1k26.gif|left|200px]]<br /><applet load="1k26" size=" | + | [[Image:1k26.gif|left|200px]]<br /><applet load="1k26" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k26, resolution 1.85Å" /> | caption="1k26, resolution 1.85Å" /> | ||
'''Structure of a Nudix Protein from Pyrobaculum aerophilum Solved by the Single Wavelength Anomolous Scattering Method'''<br /> | '''Structure of a Nudix Protein from Pyrobaculum aerophilum Solved by the Single Wavelength Anomolous Scattering Method'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nudix proteins, formerly called MutT homolog proteins, are a large family | + | Nudix proteins, formerly called MutT homolog proteins, are a large family of proteins that play an important role in reducing the accumulation of potentially toxic compounds inside the cell. They hydrolyze a wide variety of substrates that are mainly composed of a nucleoside diphosphate linked to some other moiety X and thus are called Nudix hydrolases. Here, the crystal structure of a Nudix hydrolase from the hyperthermophilic archaeon Pyrobaculum aerophilum is reported. The structure was determined by the single-wavelength anomalous scattering method with data collected at the peak anomalous wavelength of an iridium-derivatized crystal. It reveals an extensive dimer interface, with each subunit contributing two strands to the beta-sheet of the other subunit. Individual subunits consist of a mixed highly twisted and curved beta-sheet of 11 beta-strands and two alpha-helices, forming an alpha-beta-alpha sandwich. The conserved Nudix box signature motif, which contains the essential catalytic residues, is located at the first alpha-helix and the beta-strand and loop preceding it. The unusually short connections between secondary-structural elements, together with the dimer form of the structure, are likely to contribute to the thermostability of the P. aerophilum Nudix protein. |
==About this Structure== | ==About this Structure== | ||
| - | 1K26 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with SO4, IR3, NI, GOL and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1K26 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=IR3:'>IR3</scene>, <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K26 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
[[Category: Mura, C.]] | [[Category: Mura, C.]] | ||
| - | [[Category: Sawaya, M | + | [[Category: Sawaya, M R.]] |
[[Category: Wang, S.]] | [[Category: Wang, S.]] | ||
[[Category: ACY]] | [[Category: ACY]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:13 2008'' |
Revision as of 11:29, 21 February 2008
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Structure of a Nudix Protein from Pyrobaculum aerophilum Solved by the Single Wavelength Anomolous Scattering Method
Overview
Nudix proteins, formerly called MutT homolog proteins, are a large family of proteins that play an important role in reducing the accumulation of potentially toxic compounds inside the cell. They hydrolyze a wide variety of substrates that are mainly composed of a nucleoside diphosphate linked to some other moiety X and thus are called Nudix hydrolases. Here, the crystal structure of a Nudix hydrolase from the hyperthermophilic archaeon Pyrobaculum aerophilum is reported. The structure was determined by the single-wavelength anomalous scattering method with data collected at the peak anomalous wavelength of an iridium-derivatized crystal. It reveals an extensive dimer interface, with each subunit contributing two strands to the beta-sheet of the other subunit. Individual subunits consist of a mixed highly twisted and curved beta-sheet of 11 beta-strands and two alpha-helices, forming an alpha-beta-alpha sandwich. The conserved Nudix box signature motif, which contains the essential catalytic residues, is located at the first alpha-helix and the beta-strand and loop preceding it. The unusually short connections between secondary-structural elements, together with the dimer form of the structure, are likely to contribute to the thermostability of the P. aerophilum Nudix protein.
About this Structure
1K26 is a Single protein structure of sequence from Pyrobaculum aerophilum with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of a Nudix protein from Pyrobaculum aerophilum reveals a dimer with two intersubunit beta-sheets., Wang S, Mura C, Sawaya MR, Cascio D, Eisenberg D, Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):571-8. Epub 2002, Mar 22. PMID:11914479
Page seeded by OCA on Thu Feb 21 13:29:13 2008
Categories: Pyrobaculum aerophilum | Single protein | Cascio, D. | Eisenberg, D. | Mura, C. | Sawaya, M R. | Wang, S. | ACY | GOL | IR3 | NI | SO4 | Dimer | Mixed alpha/beta | Nudix/mutt-like fold | Putative nudix hydrolase | Structural genomics
