1qc7
From Proteopedia
(New page: 200px<br /><applet load="1qc7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qc7, resolution 2.2Å" /> '''T. MARITIMA FLIG C-TE...) |
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| - | [[Image:1qc7.jpg|left|200px]]<br /><applet load="1qc7" size=" | + | [[Image:1qc7.jpg|left|200px]]<br /><applet load="1qc7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qc7, resolution 2.2Å" /> | caption="1qc7, resolution 2.2Å" /> | ||
'''T. MARITIMA FLIG C-TERMINAL DOMAIN'''<br /> | '''T. MARITIMA FLIG C-TERMINAL DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many motile species of bacteria are propelled by flagella, which are rigid | + | Many motile species of bacteria are propelled by flagella, which are rigid helical filaments turned by rotary motors in the cell membrane. The motors are powered by the transmembrane gradient of protons or sodium ions. Although bacterial flagella contain many proteins, only three-MotA, MotB and FliG-participate closely in torque generation. MotA and MotB are ion-conducting membrane proteins that form the stator of the motor. FliG is a component of the rotor, present in about 25 copies per flagellum. It is composed of an amino-terminal domain that functions in flagellar assembly and a carboxy-terminal domain (FliG-C) that functions specifically in motor rotation. Here we report the crystal structure of FliG-C from the hyperthermophilic eubacterium Thermotoga maritima. Charged residues that are important for function, and which interact with the stator protein MotA, cluster along a prominent ridge on FliG-C. On the basis of the disposition of these residues, we present a hypothesis for the orientation of FliG-C domains in the flagellar motor, and propose a structural model for the part of the rotor that interacts with the stator. |
==About this Structure== | ==About this Structure== | ||
| - | 1QC7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http:// | + | 1QC7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QC7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
[[Category: Blair, D.]] | [[Category: Blair, D.]] | ||
| - | [[Category: Hill, C | + | [[Category: Hill, C P.]] |
| - | [[Category: Lloyd, S | + | [[Category: Lloyd, S A.]] |
| - | [[Category: Whitby, F | + | [[Category: Whitby, F G.]] |
[[Category: flagellar motor switch protein]] | [[Category: flagellar motor switch protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:05 2008'' |
Revision as of 12:38, 21 February 2008
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T. MARITIMA FLIG C-TERMINAL DOMAIN
Overview
Many motile species of bacteria are propelled by flagella, which are rigid helical filaments turned by rotary motors in the cell membrane. The motors are powered by the transmembrane gradient of protons or sodium ions. Although bacterial flagella contain many proteins, only three-MotA, MotB and FliG-participate closely in torque generation. MotA and MotB are ion-conducting membrane proteins that form the stator of the motor. FliG is a component of the rotor, present in about 25 copies per flagellum. It is composed of an amino-terminal domain that functions in flagellar assembly and a carboxy-terminal domain (FliG-C) that functions specifically in motor rotation. Here we report the crystal structure of FliG-C from the hyperthermophilic eubacterium Thermotoga maritima. Charged residues that are important for function, and which interact with the stator protein MotA, cluster along a prominent ridge on FliG-C. On the basis of the disposition of these residues, we present a hypothesis for the orientation of FliG-C domains in the flagellar motor, and propose a structural model for the part of the rotor that interacts with the stator.
About this Structure
1QC7 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Structure of the C-terminal domain of FliG, a component of the rotor in the bacterial flagellar motor., Lloyd SA, Whitby FG, Blair DF, Hill CP, Nature. 1999 Jul 29;400(6743):472-5. PMID:10440379
Page seeded by OCA on Thu Feb 21 14:38:05 2008
