1k2e: Difference between revisions

Revision as of 21:29, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1k2e.png

Template:STRUCTURE 1k2e

crystal structure of a nudix protein from Pyrobaculum aerophilumcrystal structure of a nudix protein from Pyrobaculum aerophilum

Template:ABSTRACT PUBMED 11914479

About this StructureAbout this Structure

1K2E is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.

ReferenceReference

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 Tue Jul 1 21:28:48 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''crystal structure of a nudix protein from Pyrobaculum aerophilum'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11914479}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11914479 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11914479}}
 ==About this Structure==
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 [[Category: Putative nudix hydrolase]]
 [[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:12:59 2008''
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