1or4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1or4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1or4, resolution 2.15&Aring;" /> '''Crystal Structure of...)
Line 1: Line 1:
-
[[Image:1or4.gif|left|200px]]<br /><applet load="1or4" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1or4.gif|left|200px]]<br /><applet load="1or4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1or4, resolution 2.15&Aring;" />
caption="1or4, resolution 2.15&Aring;" />
'''Crystal Structure of HemAT sensor domain from B.subtilis in the cyano-liganded form'''<br />
'''Crystal Structure of HemAT sensor domain from B.subtilis in the cyano-liganded form'''<br />
==Overview==
==Overview==
-
Much is now known about chemotaxis signaling transduction for Escherichia, coli and Salmonella typhimurium. The mechanism of chemotaxis of Bacillus, subtilis is, in a sense, reversed. Attractant binding strengthens the, activity of histidine kinase in B. subtilis, instead of an inhibition, reaction. The HemAT from B. subtilis can detect oxygen and transmit the, signal to regulatory proteins that control the direction of flagella, rotation. We have determined the crystal structures of the HemAT sensor, domain in liganded and unliganded forms at 2.15 A and 2.7 A resolution, respectively. The liganded structure reveals a highly symmetrical, organization. Tyrosine70 shows distinct conformational changes on one, subunit when ligands are removed. Our study suggests that disruption of, the symmetry of HemAT plays an important role in initiating the chemotaxis, signaling transduction cascade.
+
Much is now known about chemotaxis signaling transduction for Escherichia coli and Salmonella typhimurium. The mechanism of chemotaxis of Bacillus subtilis is, in a sense, reversed. Attractant binding strengthens the activity of histidine kinase in B. subtilis, instead of an inhibition reaction. The HemAT from B. subtilis can detect oxygen and transmit the signal to regulatory proteins that control the direction of flagella rotation. We have determined the crystal structures of the HemAT sensor domain in liganded and unliganded forms at 2.15 A and 2.7 A resolution, respectively. The liganded structure reveals a highly symmetrical organization. Tyrosine70 shows distinct conformational changes on one subunit when ligands are removed. Our study suggests that disruption of the symmetry of HemAT plays an important role in initiating the chemotaxis signaling transduction cascade.
==About this Structure==
==About this Structure==
-
1OR4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with CYN and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OR4 OCA].
+
1OR4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=CYN:'>CYN</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OR4 OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Jr., G.N.Phillips.]]
+
[[Category: Jr., G N.Phillips.]]
[[Category: Zhang, W.]]
[[Category: Zhang, W.]]
[[Category: CYN]]
[[Category: CYN]]
Line 19: Line 19:
[[Category: globin fold]]
[[Category: globin fold]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:07:13 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:40 2008''

Revision as of 12:20, 21 February 2008


1or4, resolution 2.15Å

Drag the structure with the mouse to rotate

Crystal Structure of HemAT sensor domain from B.subtilis in the cyano-liganded form

Overview

Much is now known about chemotaxis signaling transduction for Escherichia coli and Salmonella typhimurium. The mechanism of chemotaxis of Bacillus subtilis is, in a sense, reversed. Attractant binding strengthens the activity of histidine kinase in B. subtilis, instead of an inhibition reaction. The HemAT from B. subtilis can detect oxygen and transmit the signal to regulatory proteins that control the direction of flagella rotation. We have determined the crystal structures of the HemAT sensor domain in liganded and unliganded forms at 2.15 A and 2.7 A resolution, respectively. The liganded structure reveals a highly symmetrical organization. Tyrosine70 shows distinct conformational changes on one subunit when ligands are removed. Our study suggests that disruption of the symmetry of HemAT plays an important role in initiating the chemotaxis signaling transduction cascade.

About this Structure

1OR4 is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry., Zhang W, Phillips GN Jr, Structure. 2003 Sep;11(9):1097-110. PMID:12962628

Page seeded by OCA on Thu Feb 21 14:20:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools