2fl8: Difference between revisions

Revision as of 18:22, 21 February 2008

Fitting of the gp10 trimer structure into the cryoEM map of the bacteriophage T4 baseplate in the hexagonal conformation.

OverviewOverview

The success of tailed bacteriophages to infect cells far exceeds that of most other viruses on account of their specialized tail and associated baseplate structures. The baseplate protein gene product (gp) 10 of bacteriophage T4, whose structure was determined to 1.2 A resolution, was fitted into the cryo-electron microscopy structures of the pre and post-infection conformations of the virus. gp10 functions as a molecular lever that rotates and extends the hinged short tail fibers to facilitate cell attachment. The central folding motif of the gp10 trimer is similar to that of the baseplate protein gp11 and to the receptor-binding domain of the short tail fiber, gp12. The three proteins comprise the periphery of the baseplate and interact with each other. The structural and functional similarities of gp10, gp11, and gp12 and their sequential order in the T4 genome suggest that they evolved separately, subsequent to gene triplication from a common ancestor. Such events are usual in the evolution of complex organelles from a common primordial molecule.

About this StructureAbout this Structure

2FL8 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.

ReferenceReference

Evolution of bacteriophage tails: Structure of T4 gene product 10., Leiman PG, Shneider MM, Mesyanzhinov VV, Rossmann MG, J Mol Biol. 2006 May 5;358(3):912-21. Epub 2006 Mar 9. PMID:16554069

Page seeded by OCA on Thu Feb 21 17:22:32 2008

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OCA

@@ Line 1: / Line 1: @@
-[[Image:2fl8.gif|left|200px]]<br /><applet load="2fl8" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2fl8.gif|left|200px]]<br /><applet load="2fl8" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2fl8" />
 '''Fitting of the gp10 trimer structure into the cryoEM map of the bacteriophage T4 baseplate in the hexagonal conformation.'''<br />
 ==Overview==
-The success of tailed bacteriophages to infect cells far exceeds that of, most other viruses on account of their specialized tail and associated, baseplate structures. The baseplate protein gene product (gp) 10 of, bacteriophage T4, whose structure was determined to 1.2 A resolution, was, fitted into the cryo-electron microscopy structures of the pre and, post-infection conformations of the virus. gp10 functions as a molecular, lever that rotates and extends the hinged short tail fibers to facilitate, cell attachment. The central folding motif of the gp10 trimer is similar, to that of the baseplate protein gp11 and to the receptor-binding domain, of the short tail fiber, gp12. The three proteins comprise the periphery, of the baseplate and interact with each other. The structural and, functional similarities of gp10, gp11, and gp12 and their sequential order, in the T4 genome suggest that they evolved separately, subsequent to gene, triplication from a common ancestor. Such events are usual in the, evolution of complex organelles from a common primordial molecule.
+The success of tailed bacteriophages to infect cells far exceeds that of most other viruses on account of their specialized tail and associated baseplate structures. The baseplate protein gene product (gp) 10 of bacteriophage T4, whose structure was determined to 1.2 A resolution, was fitted into the cryo-electron microscopy structures of the pre and post-infection conformations of the virus. gp10 functions as a molecular lever that rotates and extends the hinged short tail fibers to facilitate cell attachment. The central folding motif of the gp10 trimer is similar to that of the baseplate protein gp11 and to the receptor-binding domain of the short tail fiber, gp12. The three proteins comprise the periphery of the baseplate and interact with each other. The structural and functional similarities of gp10, gp11, and gp12 and their sequential order in the T4 genome suggest that they evolved separately, subsequent to gene triplication from a common ancestor. Such events are usual in the evolution of complex organelles from a common primordial molecule.
 ==About this Structure==
-FL8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FL8 OCA].
+FL8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FL8 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bacteriophage t4]]
 [[Category: Single protein]]
-[[Category: Leiman, P.G.]]
+[[Category: Leiman, P G.]]
-[[Category: Mesyanzhinov, V.V.]]
+[[Category: Mesyanzhinov, V V.]]
-[[Category: Rossmann, M.G.]]
+[[Category: Rossmann, M G.]]
-[[Category: Shneider, M.M.]]
+[[Category: Shneider, M M.]]
 [[Category: bacteriophage t4; baseplate; tail; evolution; gp10; structural comparisons]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:36:56 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:32 2008''