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1k2e
From Proteopedia
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|PDB= 1k2e |SIZE=350|CAPTION= <scene name='initialview01'>1k2e</scene>, resolution 1.80Å | |PDB= 1k2e |SIZE=350|CAPTION= <scene name='initialview01'>1k2e</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1k26|1K26]], [[1jrk|1JRK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k2e OCA], [http://www.ebi.ac.uk/pdbsum/1k2e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k2e RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Sawaya, M R.]] | [[Category: Sawaya, M R.]] | ||
[[Category: Wang, S.]] | [[Category: Wang, S.]] | ||
| - | [[Category: ACY]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: NI]] | ||
| - | [[Category: SO4]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
| Line 37: | Line 36: | ||
[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:42:24 2008'' |
Revision as of 18:42, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1K26, 1JRK
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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