1i59
From Proteopedia
(New page: 200px<br /><applet load="1i59" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i59, resolution 1.80Å" /> '''STRUCTURE OF THE HIS...) |
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| - | [[Image:1i59.gif|left|200px]]<br /><applet load="1i59" size=" | + | [[Image:1i59.gif|left|200px]]<br /><applet load="1i59" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i59, resolution 1.80Å" /> | caption="1i59, resolution 1.80Å" /> | ||
'''STRUCTURE OF THE HISTIDINE KINASE CHEA ATP-BINDING DOMAIN IN COMPLEX WITH ADPNP AND MAGENSIUM'''<br /> | '''STRUCTURE OF THE HISTIDINE KINASE CHEA ATP-BINDING DOMAIN IN COMPLEX WITH ADPNP AND MAGENSIUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To probe the structural basis for protein histidine kinase (PHK) catalytic | + | To probe the structural basis for protein histidine kinase (PHK) catalytic activity and the prospects for PHK-specific inhibitor design, we report the crystal structures for the nucleotide binding domain of Thermotoga maritima CheA with ADP and three ATP analogs (ADPNP, ADPCP and TNP-ATP) bound with either Mg(2+) or Mn(2+). The conformation of ADPNP bound to CheA and related ATPases differs from that reported in the ADPNP complex of PHK EnvZ. Interactions of the active site with the nucleotide gamma-phosphate and its associated Mg(2+) ion are linked to conformational changes in an ATP-lid that could mediate recognition of the substrate domain. The inhibitor TNP-ATP binds CheA with its phosphates in a nonproductive conformation and its adenine and trinitrophenyl groups in two adjacent binding pockets. The trinitrophenyl interaction may be exploited for designing CheA-targeted drugs that would not interfere with host ATPases. |
==About this Structure== | ==About this Structure== | ||
| - | 1I59 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with ACT, MG, ANP and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1I59 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ANP:'>ANP</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I59 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: Bilwes, A | + | [[Category: Bilwes, A M.]] |
| - | [[Category: Crane, B | + | [[Category: Crane, B R.]] |
| - | [[Category: Croal, L | + | [[Category: Croal, L R.]] |
| - | [[Category: Quezada, C | + | [[Category: Quezada, C M.]] |
| - | [[Category: Simon, M | + | [[Category: Simon, M I.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: beta-alpha sandwich]] | [[Category: beta-alpha sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:07 2008'' |
Revision as of 11:08, 21 February 2008
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STRUCTURE OF THE HISTIDINE KINASE CHEA ATP-BINDING DOMAIN IN COMPLEX WITH ADPNP AND MAGENSIUM
Overview
To probe the structural basis for protein histidine kinase (PHK) catalytic activity and the prospects for PHK-specific inhibitor design, we report the crystal structures for the nucleotide binding domain of Thermotoga maritima CheA with ADP and three ATP analogs (ADPNP, ADPCP and TNP-ATP) bound with either Mg(2+) or Mn(2+). The conformation of ADPNP bound to CheA and related ATPases differs from that reported in the ADPNP complex of PHK EnvZ. Interactions of the active site with the nucleotide gamma-phosphate and its associated Mg(2+) ion are linked to conformational changes in an ATP-lid that could mediate recognition of the substrate domain. The inhibitor TNP-ATP binds CheA with its phosphates in a nonproductive conformation and its adenine and trinitrophenyl groups in two adjacent binding pockets. The trinitrophenyl interaction may be exploited for designing CheA-targeted drugs that would not interfere with host ATPases.
About this Structure
1I59 is a Single protein structure of sequence from Thermotoga maritima with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Nucleotide binding by the histidine kinase CheA., Bilwes AM, Quezada CM, Croal LR, Crane BR, Simon MI, Nat Struct Biol. 2001 Apr;8(4):353-60. PMID:11276258
Page seeded by OCA on Thu Feb 21 13:08:07 2008
Categories: Single protein | Thermotoga maritima | Bilwes, A M. | Crane, B R. | Croal, L R. | Quezada, C M. | Simon, M I. | ACT | ADP | ANP | MG | Beta-alpha sandwich
