1k2e
From Proteopedia
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| - | [[Image:1k2e.jpg|left|200px]] | + | [[Image:1k2e.jpg|left|200px]] |
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| - | '''crystal structure of a nudix protein from Pyrobaculum aerophilum''' | + | {{Structure |
| + | |PDB= 1k2e |SIZE=350|CAPTION= <scene name='initialview01'>1k2e</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''crystal structure of a nudix protein from Pyrobaculum aerophilum''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K2E is a [ | + | 1K2E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K2E OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11914479 11914479] |
[[Category: Pyrobaculum aerophilum]] | [[Category: Pyrobaculum aerophilum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nudix/mutt-like fold]] | [[Category: nudix/mutt-like fold]] | ||
[[Category: putative nudix hydrolase]] | [[Category: putative nudix hydrolase]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:11:38 2008'' |
Revision as of 10:11, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of a nudix protein from Pyrobaculum aerophilum
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
1K2E is a Single protein structure of sequence from Pyrobaculum aerophilum. 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
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