1id0
From Proteopedia
(New page: 200px<br /><applet load="1id0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1id0, resolution 1.60Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1id0.jpg|left|200px]]<br /><applet load="1id0" size=" | + | [[Image:1id0.jpg|left|200px]]<br /><applet load="1id0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1id0, resolution 1.60Å" /> | caption="1id0, resolution 1.60Å" /> | ||
'''CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN'''<br /> | '''CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | PhoQ is a transmembrane histidine kinase belonging to the family of | + | 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 Structure== | ==About this Structure== | ||
| - | 1ID0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1ID0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Auyzenberg, A]] | [[Category: Auyzenberg, A]] | ||
| - | [[Category: Hendrickson, W | + | [[Category: Hendrickson, W A.]] |
[[Category: Marina, A.]] | [[Category: Marina, A.]] | ||
[[Category: Mott, C.]] | [[Category: Mott, C.]] | ||
| - | [[Category: Waldburger, C | + | [[Category: Waldburger, C D.]] |
[[Category: ANP]] | [[Category: ANP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:33 2008'' |
Revision as of 11:10, 21 February 2008
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CRYSTAL STRUCTURE OF THE NUCLEOTIDE BOND CONFORMATION OF PHOQ KINASE DOMAIN
Overview
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 Structure
1ID0 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
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:11493605
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