1h5w

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[[Image:1h5w.jpg|left|200px]]
 
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{{Structure
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==2.1A Bacteriophage Phi-29 Connector==
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|PDB= 1h5w |SIZE=350|CAPTION= <scene name='initialview01'>1h5w</scene>, resolution 2.1&Aring;
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<StructureSection load='1h5w' size='340' side='right'caption='[[1h5w]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>
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<table><tr><td colspan='2'>[[1h5w]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5W FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5w OCA], [https://pdbe.org/1h5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5w RCSB], [https://www.ebi.ac.uk/pdbsum/1h5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5w ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5w OCA], [http://www.ebi.ac.uk/pdbsum/1h5w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h5w RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PORTL_BPPH2 PORTL_BPPH2] Forms the portal vertex of the capsid (PubMed:10801350) (PubMed:19744688, PubMed:21570409). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (PubMed:11812138, PubMed:21570409). Binds to the 6 packaging RNA molecules (pRNA) forming a double-ring structure which in turn binds to the ATPase gp16 hexamer, forming the active DNA-translocating motor (PubMed:15886394, PubMed:11130079). This complex is essential for the specificity of packaging from the left DNA end.[UniProtKB:P13334]<ref>PMID:11130079</ref> <ref>PMID:11812138</ref> <ref>PMID:15886394</ref> <ref>PMID:19744688</ref> <ref>PMID:21570409</ref> <ref>PMID:10801350</ref>
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<div style="background-color:#fffaf0;">
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'''2.1A BACTERIOPHAGE PHI-29 CONNECTOR'''
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== Publication Abstract from PubMed ==
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==Overview==
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The three-dimensional crystal structure of the bacteriophage phi29 connector has been solved and refined to 2.1A resolution. This 422 kDa oligomeric protein connects the head of the phage to its tail and translocates the DNA into the prohead during packaging. Each monomer has an elongated shape and is composed of a central, mainly alpha-helical domain that includes a three-helix bundle, a distal alpha/beta domain and a proximal six-stranded SH3-like domain. The protomers assemble into a 12-mer, propeller-like, super-structure with a 35 A wide central channel. The surface of the channel is mainly electronegative, but it includes two lysine rings 20 A apart. On the external surface of the particle a hydrophobic belt extends to the concave area below the SH3-like domain, which forms a crown that retains the particle in the head. The lipophilic belt contacts the non-matching symmetry vertex of the capsid and forms a bearing for the connector rotation. The structure suggests a translocation mechanism in which the longitudinal displacement of the DNA along its axis is coupled to connector spinning.
The three-dimensional crystal structure of the bacteriophage phi29 connector has been solved and refined to 2.1A resolution. This 422 kDa oligomeric protein connects the head of the phage to its tail and translocates the DNA into the prohead during packaging. Each monomer has an elongated shape and is composed of a central, mainly alpha-helical domain that includes a three-helix bundle, a distal alpha/beta domain and a proximal six-stranded SH3-like domain. The protomers assemble into a 12-mer, propeller-like, super-structure with a 35 A wide central channel. The surface of the channel is mainly electronegative, but it includes two lysine rings 20 A apart. On the external surface of the particle a hydrophobic belt extends to the concave area below the SH3-like domain, which forms a crown that retains the particle in the head. The lipophilic belt contacts the non-matching symmetry vertex of the capsid and forms a bearing for the connector rotation. The structure suggests a translocation mechanism in which the longitudinal displacement of the DNA along its axis is coupled to connector spinning.
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==About this Structure==
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Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle.,Guasch A, Pous J, Ibarra B, Gomis-Ruth FX, Valpuesta JM, Sousa N, Carrascosa JL, Coll M J Mol Biol. 2002 Jan 25;315(4):663-76. PMID:11812138<ref>PMID:11812138</ref>
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1H5W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_phi29 Bacillus phage phi29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5W OCA].
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==Reference==
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Detailed architecture of a DNA translocating machine: the high-resolution structure of the bacteriophage phi29 connector particle., Guasch A, Pous J, Ibarra B, Gomis-Ruth FX, Valpuesta JM, Sousa N, Carrascosa JL, Coll M, J Mol Biol. 2002 Jan 25;315(4):663-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11812138 11812138]
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[[Category: Bacillus phage phi29]]
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[[Category: Single protein]]
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[[Category: Carrascosa, J L.]]
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[[Category: Coll, M.]]
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[[Category: Gomis-Ruth, F X.]]
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[[Category: Guasch, A.]]
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[[Category: Ibarra, B.]]
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[[Category: Pous, J.]]
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[[Category: Sousa, N.]]
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[[Category: Valpuesta, J M.]]
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[[Category: connector]]
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[[Category: helix bundle]]
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[[Category: portal]]
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[[Category: sh3-like]]
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[[Category: virus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:25 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1h5w" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus virus phi29]]
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[[Category: Large Structures]]
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[[Category: Carrascosa JL]]
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[[Category: Coll M]]
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[[Category: Gomis-Ruth FX]]
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[[Category: Guasch A]]
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[[Category: Ibarra B]]
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[[Category: Pous J]]
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[[Category: Sousa N]]
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[[Category: Valpuesta JM]]

Current revision

2.1A Bacteriophage Phi-29 Connector

PDB ID 1h5w

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