The Structure of an ancient conserved domain establishes a structural basis for stable histidine phosphorylation and identifies a new family of adenosine-specific kinases.

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dc.contributor.author Lott, Jeremy en
dc.contributor.author Paget, BJ en
dc.contributor.author Johnston, Jodie en
dc.contributor.author Delbaere, LT en
dc.contributor.author Sigrell-simon, JA en
dc.contributor.author Banfield, MJ en
dc.contributor.author Baker, Edward en
dc.date.accessioned 2011-12-06T02:28:38Z en
dc.date.issued 2006 en
dc.identifier.citation Journal of Biological Chemistry 281 (31):22131-22141 2006 en
dc.identifier.issn 0021-9258 en
dc.identifier.uri http://hdl.handle.net/2292/9803 en
dc.description.abstract Phosphorylation of both small molecules and proteins plays a central role in many biological processes. In proteins, phosphorylation most commonly targets the oxygen atoms of Ser, Thr, and Tyr. In contrast, stably phosphorylated His residues are rarely found, due to the lability of the N-P bond, and histidine phosphorylation features most often in transient processes. Here we present the crystal structure of a protein of previously unknown function, which proves to contain a stably phosphorylated histidine residue. The protein is the product of open reading frame PAE2307, from the hyperthermophilic archaeon Pyrobaculum aerophilum, and is representative of a highly conserved protein family found in archaea and bacteria. The crystal structure of PAE2307, solved at 1.45-Å resolution (R = 0.208, Rfree = 0.227), forms a remarkably tightly associated hexamer. The phosphorylated histidine at the proposed active site, pHis85, occupies a cavity that is at the interface between two subunits and contains a number of fully conserved residues. Stable phosphorylation is attributed to favorable hydrogen bonding of the phosphoryl group and a salt bridge with pHis85 that provides electronic stabilization. In silico modeling suggested that the protein may function as an adenosine kinase, a conclusion that is supported by in vitro assays of adenosine binding, using fluorescence spectroscopy, and crystallographic visualization of an adenosine complex of PAE2307 at 2.25-Å resolution. en
dc.publisher American society for biochemistry and molecular biology en
dc.relation.ispartofseries Journal of Biological Chemistry en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/0021-9258/ en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.title The Structure of an ancient conserved domain establishes a structural basis for stable histidine phosphorylation and identifies a new family of adenosine-specific kinases. en
dc.type Journal Article en
dc.identifier.doi 10.1074/jbc.M603062200 en
pubs.begin-page 22131 en
pubs.volume 281 en
dc.rights.holder Copyright: American society for biochemistry and molecular biology en
dc.identifier.pmid 16737961 en
pubs.end-page 22141 en
dc.rights.accessrights http://purl.org/eprint/accessRights/RestrictedAccess en
pubs.subtype Article en
pubs.elements-id 96317 en
pubs.org-id Science en
pubs.org-id Biological Sciences en
pubs.org-id Science Research en
pubs.org-id Maurice Wilkins Centre (2010-2014) en
pubs.record-created-at-source-date 2010-09-01 en
pubs.dimensions-id 16737961 en


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