1g3p: Difference between revisions

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-[[Image:1g3p.gif|left|200px]]
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-{{STRUCTURE_1g3p|  PDB=1g3p  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAINS OF BACTERIOPHAGE MINOR COAT PROTEIN G3P'''
+==CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAINS OF BACTERIOPHAGE MINOR COAT PROTEIN G3P==
+<StructureSection load='1g3p' size='340' side='right'caption='[[1g3p]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1g3p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_M13 Escherichia virus M13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G3P FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.46&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRO:2-HYDROXY-TRYPTOPHAN'>TRO</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g3p OCA], [https://pdbe.org/1g3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g3p RCSB], [https://www.ebi.ac.uk/pdbsum/1g3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g3p ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/G3P_BPM13 G3P_BPM13] Plays essential roles both in the penetration of the viral genome into the bacterial host via pilus retraction and in the extrusion process. During the initial step of infection, G3P mediates adsorption of the phage to its primary receptor, the tip of host F-pilus. Subsequent interaction with the host entry receptor tolA induces penetration of the viral DNA into the host cytoplasm. In the extrusion process, G3P mediates the release of the membrane-anchored virion from the cell via its C-terminal domain.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==Overview==
+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<ref>PMID:9461080</ref>
-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==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-G3P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_m13 Enterobacteria phage m13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3P OCA].
+</div>
+<div class="pdbe-citations 1g3p" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/9461080 9461080]
+*[[G3p|G3p]]
-[[Category: Enterobacteria phage m13]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Hennecke, F.]]
+__TOC__
-[[Category: Lubkowski, J.]]
+</StructureSection>
-[[Category: Pluckthun, A.]]
+[[Category: Escherichia virus M13]]
-[[Category: Wlodawer, A.]]
+[[Category: Large Structures]]
-[[Category: Filamentous bacteriophage]]
+[[Category: Hennecke F]]
-[[Category: Minor coat protein]]
+[[Category: Lubkowski J]]
-[[Category: Phage display]]
+[[Category: Pluckthun A]]
-[[Category: Selectively infective phage]]
+[[Category: Wlodawer A]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:05:57 2008''