2fkk: Difference between revisions

Revision as of 18:22, 21 February 2008

Crystal structure of the C-terminal domain of the bacteriophage T4 gene product 10

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

2FKK is a Single protein structure of sequence from Bacteriophage t4 with , , and as ligands. 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 17:22:20 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2fkk.gif|left|200px]]<br /><applet load="2fkk" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2fkk.gif|left|200px]]<br /><applet load="2fkk" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2fkk, resolution 1.2&Aring;" />
 '''Crystal structure of the C-terminal domain of the bacteriophage T4 gene product 10'''<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==
-FKK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with BR, PO3, TRS and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FKK OCA].
+FKK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=BR:'>BR</scene>, <scene name='pdbligand=PO3:'>PO3</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FKK 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: BR]]
 [[Category: EDO]]
@@ Line 23: / Line 23: @@
 [[Category: bacteriophage t4; baseplate; tail; evolution; gp10; structural comparisons]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:36:23 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:20 2008''