1g3p

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(New page: 200px<br /><applet load="1g3p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g3p, resolution 1.46&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1g3p.gif|left|200px]]<br /><applet load="1g3p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g3p, resolution 1.46&Aring;" />
caption="1g3p, resolution 1.46&Aring;" />
'''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAINS OF BACTERIOPHAGE MINOR COAT PROTEIN G3P'''<br />
'''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAINS OF BACTERIOPHAGE MINOR COAT PROTEIN G3P'''<br />
==Overview==
==Overview==
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The structure of the two N-terminal domains of the gene 3 protein of, filamentous phages (residues 1-217) has been solved by multiwavelength, anomalous diffraction and refined at 1.46 A resolution. Each domain, consists of either five or eight beta-strands and a single alpha-helix., Despite missing sequence homology, their cores superimposed with a, root-mean-square deviation of 2 A. The domains are engaged in extensive, interactions, resulting in a horseshoe shape with aliphatic amino acids, and threonines lining the inside, delineating the likely binding site for, the F-pilus. The glycine-rich linker connecting the domains is invisible, in the otherwise highly ordered structure and may confer flexibility, between the domains required during the infection process.
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The structure of the two N-terminal domains of the gene 3 protein of filamentous phages (residues 1-217) has been solved by multiwavelength anomalous diffraction and refined at 1.46 A resolution. Each domain consists of either five or eight beta-strands and a single alpha-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 A. The domains are engaged in extensive interactions, resulting in a horseshoe shape with aliphatic amino acids and threonines lining the inside, delineating the likely binding site for the F-pilus. The glycine-rich linker connecting the domains is invisible in the otherwise highly ordered structure and may confer flexibility between the domains required during the infection process.
==About this Structure==
==About this Structure==
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1G3P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G3P OCA].
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1G3P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3P OCA].
==Reference==
==Reference==
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[[Category: selectively infective phages]]
[[Category: selectively infective phages]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:40:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:43 2008''

Revision as of 10:45, 21 February 2008


1g3p, resolution 1.46Å

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CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAINS OF BACTERIOPHAGE MINOR COAT PROTEIN G3P

Overview

The structure of the two N-terminal domains of the gene 3 protein of filamentous phages (residues 1-217) has been solved by multiwavelength anomalous diffraction and refined at 1.46 A resolution. Each domain consists of either five or eight beta-strands and a single alpha-helix. Despite missing sequence homology, their cores superimposed with a root-mean-square deviation of 2 A. The domains are engaged in extensive interactions, resulting in a horseshoe shape with aliphatic amino acids and threonines lining the inside, delineating the likely binding site for the F-pilus. The glycine-rich linker connecting the domains is invisible in the otherwise highly ordered structure and may confer flexibility between the domains required during the infection process.

About this Structure

1G3P is a Single protein structure of sequence from Enterobacteria phage mu with as ligand. Full crystallographic information is available from OCA.

Reference

The structural basis of phage display elucidated by the crystal structure of the N-terminal domains of g3p., Lubkowski J, Hennecke F, Pluckthun A, Wlodawer A, Nat Struct Biol. 1998 Feb;5(2):140-7. PMID:9461080

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