2gl0

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[[Image:2gl0.gif|left|200px]]<br /><applet load="2gl0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2gl0.gif|left|200px]]
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caption="2gl0, resolution 2.250&Aring;" />
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'''Structure of PAE2307 in complex with adenosine'''<br />
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{{Structure
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|PDB= 2gl0 |SIZE=350|CAPTION= <scene name='initialview01'>2gl0</scene>, resolution 2.250&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20]
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|GENE= PAE2307 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum])
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}}
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'''Structure of PAE2307 in complex with adenosine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2GL0 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=PO4:'>PO4</scene> and <scene name='pdbligand=ADN:'>ADN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GL0 OCA].
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2GL0 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=2GL0 OCA].
==Reference==
==Reference==
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The structure of an ancient conserved domain establishes a structural basis for stable histidine phosphorylation and identifies a new family of adenosine-specific kinases., Lott JS, Paget B, Johnston JM, Delbaere LT, Sigrell-Simon JA, Banfield MJ, Baker EN, J Biol Chem. 2006 Aug 4;281(31):22131-41. Epub 2006 May 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16737961 16737961]
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The structure of an ancient conserved domain establishes a structural basis for stable histidine phosphorylation and identifies a new family of adenosine-specific kinases., Lott JS, Paget B, Johnston JM, Delbaere LT, Sigrell-Simon JA, Banfield MJ, Baker EN, J Biol Chem. 2006 Aug 4;281(31):22131-41. Epub 2006 May 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16737961 16737961]
[[Category: Adenosine kinase]]
[[Category: Adenosine kinase]]
[[Category: Pyrobaculum aerophilum]]
[[Category: Pyrobaculum aerophilum]]
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[[Category: putative kinase]]
[[Category: putative kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:06:00 2008''

Revision as of 15:06, 20 March 2008


PDB ID 2gl0

Drag the structure with the mouse to rotate
, resolution 2.250Å
Ligands: and
Gene: PAE2307 (Pyrobaculum aerophilum)
Activity: Adenosine kinase, with EC number 2.7.1.20
Coordinates: save as pdb, mmCIF, xml



Structure of PAE2307 in complex with adenosine


Overview

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-A resolution (R = 0.208, R(free) = 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-A resolution.

About this Structure

2GL0 is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.

Reference

The structure of an ancient conserved domain establishes a structural basis for stable histidine phosphorylation and identifies a new family of adenosine-specific kinases., Lott JS, Paget B, Johnston JM, Delbaere LT, Sigrell-Simon JA, Banfield MJ, Baker EN, J Biol Chem. 2006 Aug 4;281(31):22131-41. Epub 2006 May 30. PMID:16737961

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