G3p: Difference between revisions

Line 16:

One year later, another structure containing D1 and D2 (albeit from the filamentous phage, fd, containing a two residue difference) was published using x-ray crystallography to 1.9Å resolution <ref name="holliger 99"/>. Dimer formation was observed, but was attributed to the experimental conditions.

Finally, two papers <ref name="lubkowski 99"> PMID: 10404600 </ref> <ref name="deprez"> PMID:15701516 </ref> were later published described interactions between g3p and TolA protein (located on the host cell, see [[Infectivity]].

Finally, two papers <ref name="lubkowski 99"> PMID: 10404600 </ref> <ref name="deprez"> PMID:15701516 </ref> were later published described interactions between g3p and TolA protein (located on the host cell, see [[#Infectivity]].

===D1 Domain===

Line 37:

==Functional Implications==

===Infectivity===

The function of the protein has a close correlation with its structural domains. The D1 domain interacts with TolA protein in the periplasm of the bacterial cell. <ref name="lubkowski"/><ref name="cabilly"/><ref name="holliger 99"/>. (The C terminal domain of TolA is the coreceptor for filamentous phage infection of E coli(Cell 90, 351-360 (1997)). The D2 domain binds to F pilus on the outer membrane of ''Escherichia coli'', however, it is also blocks TolA binding to D1 in the absence of the F pilus <ref name="chatellier"> PMID:10606756 </ref>. In fact, without the D2 domain, infectivity is very low<ref name="lubkowski"/>. It has been speculated that D2 interacts with the F pilus first, drawing the phage closer to the bacterial cell, thus allowing D1-TolA interactions to occur<ref name="holliger 99"/>. Chatellier et al suggest that the complex formed by D1 and D2 may prevent destruction of the protein from bacterial proteases, and upon binding the protein opens up and D3 can then reach the inner membrane of the bacteria<ref name="chatellier"/>.

The function of the protein has a close correlation with its structural domains. The <scene name='G3p/D1_and_tola/1'>D1 domain (blue) interacts with TolA protein (orange)</scene> in the periplasm of the bacterial cell. <ref name="lubkowski"/><ref name="cabilly"/><ref name="holliger 99"/>. (The C terminal domain of TolA is the coreceptor for filamentous phage infection of E coli(Cell 90, 351-360 (1997)). The D2 domain binds to F pilus on the outer membrane of ''Escherichia coli'', however, it is also blocks TolA binding to D1 in the absence of the F pilus <ref name="chatellier"> PMID:10606756 </ref>. In fact, without the D2 domain, infectivity is very low<ref name="lubkowski"/>. It has been speculated that D2 interacts with the F pilus first, drawing the phage closer to the bacterial cell, thus allowing D1-TolA interactions to occur<ref name="holliger 99"/>. Chatellier et al suggest that the complex formed by D1 and D2 may prevent destruction of the protein from bacterial proteases, and upon binding the protein opens up and D3 can then reach the inner membrane of the bacteria<ref name="chatellier"/>.

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@@ Line 16: / Line 16: @@
 One year later, another structure containing D1 and D2 (albeit from the filamentous phage, fd, containing a two residue difference) was published using x-ray crystallography to 1.9Å resolution <ref name="holliger 99"/>. Dimer formation was observed, but was attributed to the experimental conditions.
-Finally, two papers <ref name="lubkowski 99"> PMID: 10404600 </ref> <ref name="deprez"> PMID:15701516 </ref> were later published described interactions between g3p and TolA protein (located on the host cell, see [[Infectivity]].
+Finally, two papers <ref name="lubkowski 99"> PMID: 10404600 </ref> <ref name="deprez"> PMID:15701516 </ref> were later published described interactions between g3p and TolA protein (located on the host cell, see [[#Infectivity]].
 ===D1 Domain===
@@ Line 37: / Line 37: @@
 ==Functional Implications==
 ===Infectivity===
-{{STRUCTURE_1tol |  PDB=1tol  |  SCENE=  }}
+<applet load='{{STRUCTURE_1tol |  PDB=1tol  |  SCENE=  }}' size='300' frame='true' align='right' caption='Insert caption here' />
-The function of the protein has a close correlation with its structural domains. The D1 domain interacts with TolA protein in the periplasm of the bacterial cell. <ref name="lubkowski"/><ref name="cabilly"/><ref name="holliger 99"/>. (The C terminal domain of TolA is the coreceptor for filamentous phage infection of E coli(Cell 90, 351-360 (1997)). The D2 domain binds to F pilus on the outer membrane of ''Escherichia coli'', however, it is also blocks TolA binding to D1 in the absence of the F pilus <ref name="chatellier"> PMID:10606756 </ref>. In fact, without the D2 domain, infectivity is very low<ref name="lubkowski"/>. It has been speculated that D2 interacts with the F pilus first, drawing the phage closer to the bacterial cell, thus allowing D1-TolA interactions to occur<ref name="holliger 99"/>.  Chatellier et al suggest that the complex formed by D1 and D2 may prevent destruction of the protein from bacterial proteases, and upon binding the protein opens up and D3 can then reach the inner membrane of the bacteria<ref name="chatellier"/>.
+The function of the protein has a close correlation with its structural domains. The <scene name='G3p/D1_and_tola/1'>D1 domain (blue) interacts with TolA protein (orange)</scene> in the periplasm of the bacterial cell. <ref name="lubkowski"/><ref name="cabilly"/><ref name="holliger 99"/>. (The C terminal domain of TolA is the coreceptor for filamentous phage infection of E coli(Cell 90, 351-360 (1997)). The D2 domain binds to F pilus on the outer membrane of ''Escherichia coli'', however, it is also blocks TolA binding to D1 in the absence of the F pilus <ref name="chatellier"> PMID:10606756 </ref>. In fact, without the D2 domain, infectivity is very low<ref name="lubkowski"/>. It has been speculated that D2 interacts with the F pilus first, drawing the phage closer to the bacterial cell, thus allowing D1-TolA interactions to occur<ref name="holliger 99"/>.  Chatellier et al suggest that the complex formed by D1 and D2 may prevent destruction of the protein from bacterial proteases, and upon binding the protein opens up and D3 can then reach the inner membrane of the bacteria<ref name="chatellier"/>.