2gl0: Difference between revisions
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|PDB= 2gl0 |SIZE=350|CAPTION= <scene name='initialview01'>2gl0</scene>, resolution 2.250Å | |PDB= 2gl0 |SIZE=350|CAPTION= <scene name='initialview01'>2gl0</scene>, resolution 2.250Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | ||
|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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= PAE2307 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum]) | |GENE= PAE2307 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1wvq|1WVQ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gl0 OCA], [http://www.ebi.ac.uk/pdbsum/2gl0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gl0 RCSB]</span> | |||
}} | }} | ||
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[[Category: Lott, J S.]] | [[Category: Lott, J S.]] | ||
[[Category: Paget, B.]] | [[Category: Paget, B.]] | ||
[[Category: histidine phosphorylation]] | [[Category: histidine phosphorylation]] | ||
[[Category: protein-adenosine complex]] | [[Category: protein-adenosine complex]] | ||
[[Category: putative kinase]] | [[Category: putative kinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:17:59 2008'' | ||
Revision as of 03:18, 31 March 2008
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| , resolution 2.250Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | PAE2307 (Pyrobaculum aerophilum) | ||||||
| Activity: | Adenosine kinase, with EC number 2.7.1.20 | ||||||
| Related: | 1WVQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of PAE2307 in complex with adenosine
OverviewOverview
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 StructureAbout this Structure
2GL0 is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.
ReferenceReference
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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