1fou

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{{Seed}}
 
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[[Image:1fou.png|left|200px]]
 
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==CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29==
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The line below this paragraph, containing "STRUCTURE_1fou", creates the "Structure Box" on the page.
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<StructureSection load='1fou' size='340' side='right'caption='[[1fou]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1fou]] is a 12 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=1FOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOU FirstGlance]. <br>
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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]] 3.2&#8491;</td></tr>
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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=1fou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fou OCA], [https://pdbe.org/1fou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fou RCSB], [https://www.ebi.ac.uk/pdbsum/1fou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fou ProSAT]</span></td></tr>
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{{STRUCTURE_1fou| PDB=1fou | SCENE= }}
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</table>
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== Function ==
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===CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29===
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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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== References ==
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<references/>
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 11130079 is the PubMed ID number.
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[[Category: Bacillus virus phi29]]
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[[Category: Large Structures]]
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{{ABSTRACT_PUBMED_11130079}}
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[[Category: Anderson DL]]
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[[Category: Badasso MO]]
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==About this Structure==
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[[Category: Baker TS]]
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1FOU 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=1FOU OCA].
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[[Category: Grimes SN]]
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[[Category: He Y]]
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==Reference==
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[[Category: Jardine PJ]]
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Structure of the bacteriophage phi29 DNA packaging motor., Simpson AA, Tao Y, Leiman PG, Badasso MO, He Y, Jardine PJ, Olson NH, Morais MC, Grimes S, Anderson DL, Baker TS, Rossmann MG, Nature. 2000 Dec 7;408(6813):745-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11130079 11130079]
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[[Category: Leiman PG]]
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[[Category: Bacillus phage phi29]]
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[[Category: Morais MC]]
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[[Category: Single protein]]
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[[Category: Olson NH]]
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[[Category: Anderson, D L.]]
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[[Category: Rossmann MG]]
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[[Category: Badasso, M O.]]
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[[Category: Simpson AA]]
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[[Category: Baker, T S.]]
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[[Category: Tao Y]]
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[[Category: Grimes, S N.]]
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[[Category: He, Y.]]
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[[Category: Jardine, P J.]]
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[[Category: Leiman, P G.]]
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[[Category: Morais, M C.]]
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[[Category: Olson, N H.]]
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[[Category: Rossmann, M G.]]
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[[Category: Simpson, A A.]]
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[[Category: Tao, Y.]]
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[[Category: Alpha-helical barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:42:17 2008''
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Current revision

CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29

PDB ID 1fou

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