1id0: Difference between revisions
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[[Image:1id0.jpg|left|200px]] | [[Image:1id0.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN''' | {{Structure | ||
|PDB= 1id0 |SIZE=350|CAPTION= <scene name='initialview01'>1id0</scene>, resolution 1.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ID0 is a [ | 1ID0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID0 OCA]. | ||
==Reference== | ==Reference== | ||
Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism., Marina A, Mott C, Auyzenberg A, Hendrickson WA, Waldburger CD, J Biol Chem. 2001 Nov 2;276(44):41182-90. Epub 2001 Aug 7. PMID:[http:// | Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism., Marina A, Mott C, Auyzenberg A, Hendrickson WA, Waldburger CD, J Biol Chem. 2001 Nov 2;276(44):41182-90. Epub 2001 Aug 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11493605 11493605] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:42 2008'' | ||
Revision as of 12:48, 20 March 2008
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| , resolution 1.60Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN
OverviewOverview
PhoQ is a transmembrane histidine kinase belonging to the family of two-component signal transducing systems common in prokaryotes and lower eukaryotes. In response to changes in environmental Mg(2+) concentration, PhoQ regulates the level of phosphorylated PhoP, its cognate transcriptional response-regulator. The PhoQ cytoplasmic region comprises two independently folding domains: the histidine-containing phosphotransfer domain and the ATP-binding kinase domain. We have determined the structure of the kinase domain of Escherichia coli PhoQ complexed with the non-hydrolyzable ATP analog adenosine 5'-(beta,gamma-imino)triphosphate and Mg(2+). Nucleotide binding appears to be accompanied by conformational changes in the loop that surrounds the ATP analog (ATP-lid) and has implications for interactions with the substrate phosphotransfer domain. The high resolution (1.6 A) structure reveals a detailed view of the nucleotide-binding site, allowing us to identify potential catalytic residues. Mutagenic analyses of these residues provide new insights into the catalytic mechanism of histidine phosphorylation in the histidine kinase family. Comparison with the active site of the related GHL ATPase family reveals differences that are proposed to account for the distinct functions of these proteins.
About this StructureAbout this Structure
1ID0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism., Marina A, Mott C, Auyzenberg A, Hendrickson WA, Waldburger CD, J Biol Chem. 2001 Nov 2;276(44):41182-90. Epub 2001 Aug 7. PMID:11493605
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