5gai

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{{Large structure}}
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==Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins==
==Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins==
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<StructureSection load='5gai' size='340' side='right' caption='[[5gai]], [[Resolution|resolution]] 10.50&Aring;' scene=''>
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<StructureSection load='5gai' size='340' side='right'caption='[[5gai]], [[Resolution|resolution]] 10.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5gai]] is a 27 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GAI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GAI FirstGlance]. <br>
<table><tr><td colspan='2'>[[5gai]] is a 27 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GAI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GAI FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gai OCA], [http://pdbe.org/5gai PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gai RCSB], [http://www.ebi.ac.uk/pdbsum/5gai PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gai ProSAT]</span></td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gai OCA], [http://pdbe.org/5gai PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gai RCSB], [http://www.ebi.ac.uk/pdbsum/5gai PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gai ProSAT]</span></td></tr>
</table>
</table>
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{{Large structure}}
 
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PORTL_BPP22 PORTL_BPP22]] Required for successful condensation of DNA within the capsid. Gp1 is a minor structural protein. The portal protein is present as a single ring-shaped dodecamer located at the point where tails attach. It is through this ring that DNA is thought to enter the prohead. [[http://www.uniprot.org/uniprot/FIBER_BPP22 FIBER_BPP22]] Structural component of the short non-contractile tail. The tail comprises six fibers that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.<ref>PMID:12837775</ref> <ref>PMID:20817910</ref> [[http://www.uniprot.org/uniprot/EXLYS_BPP22 EXLYS_BPP22]] Tail protein located at the vertex occupied by the portal ring. Together with gp10 and gp26, gp4 is required for stabilization of the condensed DNA within the capsid; perhaps by plugging the hole through which the DNA enters. Plays a role in ejection of the bacteriophage DNA into the host cell at the initiation of infection. Functions as an exolysin that catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycans.<ref>PMID:14763988</ref>
[[http://www.uniprot.org/uniprot/PORTL_BPP22 PORTL_BPP22]] Required for successful condensation of DNA within the capsid. Gp1 is a minor structural protein. The portal protein is present as a single ring-shaped dodecamer located at the point where tails attach. It is through this ring that DNA is thought to enter the prohead. [[http://www.uniprot.org/uniprot/FIBER_BPP22 FIBER_BPP22]] Structural component of the short non-contractile tail. The tail comprises six fibers that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.<ref>PMID:12837775</ref> <ref>PMID:20817910</ref> [[http://www.uniprot.org/uniprot/EXLYS_BPP22 EXLYS_BPP22]] Tail protein located at the vertex occupied by the portal ring. Together with gp10 and gp26, gp4 is required for stabilization of the condensed DNA within the capsid; perhaps by plugging the hole through which the DNA enters. Plays a role in ejection of the bacteriophage DNA into the host cell at the initiation of infection. Functions as an exolysin that catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycans.<ref>PMID:14763988</ref>
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</StructureSection>
</StructureSection>
[[Category: Bpp22]]
[[Category: Bpp22]]
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[[Category: Large Structures]]
[[Category: Chen, D H]]
[[Category: Chen, D H]]
[[Category: Chiu, W]]
[[Category: Chiu, W]]

Revision as of 16:11, 11 December 2019

Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins

PDB ID 5gai

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