1ujc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ujc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ujc, resolution 1.90&Aring;" /> '''Structure of the pro...)
Line 1: Line 1:
-
[[Image:1ujc.gif|left|200px]]<br /><applet load="1ujc" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ujc.gif|left|200px]]<br /><applet load="1ujc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ujc, resolution 1.90&Aring;" />
caption="1ujc, resolution 1.90&Aring;" />
'''Structure of the protein histidine phosphatase SixA complexed with tungstate'''<br />
'''Structure of the protein histidine phosphatase SixA complexed with tungstate'''<br />
==Overview==
==Overview==
-
The multiple histidine-aspartate phosphorelay system plays a crucial role, in cellular adaptation to environments in microorganisms and plants. Like, kinase-phosphatase systems in higher eukaryotes, the multiple steps, provide additional regulatory checkpoints with phosphatases. The, Escherichia coli phosphatase SixA exhibits protein phosphatase activity, against the histidine-containing phosphotransfer (HPt) domain located in, the C-terminus of the histidine kinase ArcB engaged in anaerobic, responses. We have determined the crystal structures of the free and, tungstate-bound forms of SixA at 2.06 A and 1.90 A resolution, respectively. The results provide the first three-dimensional view of a, bacterial protein histidine phosphatase, revealing a compact alpha/beta, architecture related to a family of phosphatases containing the, arginine-histidine-glycine (RHG) motif at their active sites. Compared, with these RHG phosphatases, SixA lacks an extra alpha-helical subdomain, as a lid over the active site, thereby forming a relatively shallow groove, important for the accommodation of the HPt domain of ArcB. The tungstate, ion, which mimics the substrate phosphate group, is located at the centre, of the active site where the active residue, His8, points to the tungsten, atom in the mode of in-line nucleophilic attack.
+
The multiple histidine-aspartate phosphorelay system plays a crucial role in cellular adaptation to environments in microorganisms and plants. Like kinase-phosphatase systems in higher eukaryotes, the multiple steps provide additional regulatory checkpoints with phosphatases. The Escherichia coli phosphatase SixA exhibits protein phosphatase activity against the histidine-containing phosphotransfer (HPt) domain located in the C-terminus of the histidine kinase ArcB engaged in anaerobic responses. We have determined the crystal structures of the free and tungstate-bound forms of SixA at 2.06 A and 1.90 A resolution, respectively. The results provide the first three-dimensional view of a bacterial protein histidine phosphatase, revealing a compact alpha/beta architecture related to a family of phosphatases containing the arginine-histidine-glycine (RHG) motif at their active sites. Compared with these RHG phosphatases, SixA lacks an extra alpha-helical subdomain as a lid over the active site, thereby forming a relatively shallow groove important for the accommodation of the HPt domain of ArcB. The tungstate ion, which mimics the substrate phosphate group, is located at the centre of the active site where the active residue, His8, points to the tungsten atom in the mode of in-line nucleophilic attack.
==About this Structure==
==About this Structure==
-
1UJC 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 CA and WO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UJC OCA].
+
1UJC 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=CA:'>CA</scene> and <scene name='pdbligand=WO4:'>WO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UJC OCA].
==Reference==
==Reference==
Line 23: Line 23:
[[Category: alpha-beta fold]]
[[Category: alpha-beta fold]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:10:38 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:12 2008''

Revision as of 13:25, 21 February 2008

Image:1ujc.gif

1ujc, resolution 1.90Å

Drag the structure with the mouse to rotate

Structure of the protein histidine phosphatase SixA complexed with tungstate

Overview

The multiple histidine-aspartate phosphorelay system plays a crucial role in cellular adaptation to environments in microorganisms and plants. Like kinase-phosphatase systems in higher eukaryotes, the multiple steps provide additional regulatory checkpoints with phosphatases. The Escherichia coli phosphatase SixA exhibits protein phosphatase activity against the histidine-containing phosphotransfer (HPt) domain located in the C-terminus of the histidine kinase ArcB engaged in anaerobic responses. We have determined the crystal structures of the free and tungstate-bound forms of SixA at 2.06 A and 1.90 A resolution, respectively. The results provide the first three-dimensional view of a bacterial protein histidine phosphatase, revealing a compact alpha/beta architecture related to a family of phosphatases containing the arginine-histidine-glycine (RHG) motif at their active sites. Compared with these RHG phosphatases, SixA lacks an extra alpha-helical subdomain as a lid over the active site, thereby forming a relatively shallow groove important for the accommodation of the HPt domain of ArcB. The tungstate ion, which mimics the substrate phosphate group, is located at the centre of the active site where the active residue, His8, points to the tungsten atom in the mode of in-line nucleophilic attack.

About this Structure

1UJC is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the protein histidine phosphatase SixA in the multistep His-Asp phosphorelay., Hamada K, Kato M, Shimizu T, Ihara K, Mizuno T, Hakoshima T, Genes Cells. 2005 Jan;10(1):1-11. PMID:15670209

Page seeded by OCA on Thu Feb 21 15:25:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ujc"
Personal tools