G3p: Difference between revisions

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[[Image:wt_and_pIII.jpg |frame|right|Figure Adapted from Hill and Stockley et al, 1996 <ref name="hill"> PMID:8793867 </ref>]]  
[[Image:wt_and_pIII.jpg |frame|right|Figure Adapted from Hill and Stockley et al, 1996 <ref name="hill"> PMID:8793867 </ref>]]  
Gene 3 protein (g3p pr pIII) is a minor coat protein found on the surface of filamentous bacteriophage <ref name="lubkowski"> PMID:9461080 </ref>.  The protein consists of 406 amino acids divided into three domains interspaced with glycine linkers <ref name="lubkowski"/> <ref name="cabilly"> PMID:10596371 </ref>.  Peptides or proteins can be fused to g3p and evaluated for binding or other properties.   
Gene 3 protein (g3p pr pIII) is a minor coat protein found on the surface of filamentous bacteriophage <ref name="lubkowski"> PMID:9461080 </ref>.  The protein consists of 406 amino acids divided into three domains interspaced with glycine linkers <ref name="lubkowski"/> <ref name="cabilly"> PMID:10596371 </ref>.  Peptides or proteins can be fused to g3p and evaluated for binding or other properties.   
 
[[Image:F1_holliger_and_riechmann.jpg |frame|center|Figure Adapted from Holliger and Riechmann, 1997<ref name="holliger 97"> PMID:9032075 </ref>]]
 
 


==Structural Analysis==
==Structural Analysis==
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===Initial Observations===
===Initial Observations===
<applet load='1fgp' size='150' frame='true' align='left' caption='Initial structure of D1' />The first structure of g3p entered into the PDB was by Holliger and Riechmann in late 1996-early 1997<ref name="holliger 97"> PMID:9032075 </ref>.  They used NMR spectroscopy to create a structure of the first domains of g3p.  Shown is a combination of the 15 most energetically favorable states. Observations of secondary structure are below.
<applet load='1fgp' size='150' frame='true' align='left' caption='Initial structure of D1' />The first structure of g3p entered into the PDB was by Holliger and Riechmann in late 1996-early 1997<ref name="holliger 97"/>.  They used NMR spectroscopy to create a structure of the first domains of g3p.  Shown is a combination of the 15 most energetically favorable states. Observations of secondary structure are below.
<applet load='1g3p' size='300' frame='true' align='right' caption='Important characteristics of the N-terminal domains of g3p' />
<applet load='1g3p' size='300' frame='true' align='right' caption='Important characteristics of the N-terminal domains of g3p' />


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===N2 domain===
===N2 domain===
- 8 beta strands, 6 in a mixed beta sheet, 2 interacting with N2 antiparallel sheet <ref name="lubkowski"/>
This domain contains eight beta strands: six in a mixed beta sheet and two interacting with D1 antiparallel sheet (β6 and β13 <ref name="lubkowski"/>. The amino acids between β6 and β7 doesn’t have a specific motif but has stabilizing hydrophobic interactions with other parts of the domain <ref name="lubkowski"/>. Three hairpins exist in this domain: between β8 and β9, β9 and β10, and β10 and β11 (cis proline in the last hairpin) <ref name="lubkowski"/>.  The final secondary structural element is an alpha helix that interacts with rest of the domain via hydrophobic interactions <ref name="lubkowski"/>. Of note, there is a cation-π interaction between His 191 and Phe 199. The C terminus of D2 has seven peptides, 3 of which are proline, 1 of which is <scene name='G3p/Pro_213_in_cis_conformation/1'>in the cis conformation</scene> <ref name="lubkowski"/>.
Strand between B6 and B7 doesn’t have a specific motif but contributes via stabilizing hydrophobic interactions <ref name="lubkowski"/>
3 hairpins between 8 and 9, 9 and 10, and 10 and 11 (cis proline in the last hairpin) <ref name="lubkowski"/>
One alpha helix that interacts with rest of N2 domain by hydrophobic interactions <ref name="lubkowski"/>
Cation pi interaction between His 191 and Phe 199
C terminus of N2 has seven peptides, 3 of which are proline, 1 of which is in the cis conformation
   
   
{{STRUCTURE_2g3p |  PDB=2g3p  |  SCENE=  }}
{{STRUCTURE_2g3p |  PDB=2g3p  |  SCENE=  }}