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2bsg

From Proteopedia

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Current revision

The modeled structure of fibritin (gpwac) of bacteriophage T4 based on cryo-EM reconstruction of the extended tail of bacteriophage T4

2bsg, resolution 15.00Å

Structural highlights

2bsg is a 3 chain structure with sequence from Escherichia virus T4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 15Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

WAC_BPT4 Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail assembly at 15-A resolution shows the hexagonal dome-shaped baseplate, the extended contractile sheath, the long tail fibers attached to the baseplate and the collar formed by six whiskers that interact with the long tail fibers. Comparison with the structure of the contracted tail shows that tail contraction is associated with a substantial rearrangement of the domains within the sheath protein and results in shortening of the sheath to about one-third of its original length. During contraction, the tail tube extends beneath the baseplate by about one-half of its total length and rotates by 345 degrees , allowing it to cross the host's periplasmic space.

The tail structure of bacteriophage T4 and its mechanism of contraction.,Kostyuchenko VA, Chipman PR, Leiman PG, Arisaka F, Mesyanzhinov VV, Rossmann MG Nat Struct Mol Biol. 2005 Sep;12(9):810-3. Epub 2005 Aug 14. PMID:16116440^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kostyuchenko VA, Chipman PR, Leiman PG, Arisaka F, Mesyanzhinov VV, Rossmann MG. The tail structure of bacteriophage T4 and its mechanism of contraction. Nat Struct Mol Biol. 2005 Sep;12(9):810-3. Epub 2005 Aug 14. PMID:16116440 doi:10.1038/nsmb975

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bsg"

@@ Line 3: / Line 3: @@
 <SX load='2bsg' size='340' side='right' viewer='molstar' caption='[[2bsg]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bsg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BSG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bsg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BSG FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aa0|1aa0]], [[1avy|1avy]], [[1ox3|1ox3]], [[1rfo|1rfo]], [[1v1h|1v1h]], [[1v1i|1v1i]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 15&#8491;</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=2bsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsg OCA], [https://pdbe.org/2bsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bsg RCSB], [https://www.ebi.ac.uk/pdbsum/2bsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsg ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4]] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').
+[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 35: @@
 __TOC__
 </SX>
-[[Category: Bacteriophage t4]]
+[[Category: Escherichia virus T4]]
 [[Category: Large Structures]]
-[[Category: Arisaka, F]]
+[[Category: Arisaka F]]
-[[Category: Chipman, P R]]
+[[Category: Chipman PR]]
-[[Category: Kostyuchenko, V A]]
+[[Category: Kostyuchenko VA]]
-[[Category: Leiman, P G]]
+[[Category: Leiman PG]]
-[[Category: Mesyanzhinov, V V]]
+[[Category: Mesyanzhinov VV]]
-[[Category: Rossmann, M G]]
+[[Category: Rossmann MG]]
-[[Category: Attachment protein]]
-[[Category: Bacteriophage assembly]]
-[[Category: Chaperone]]
-[[Category: Fibritin]]
-[[Category: Structural protein]]
-[[Category: Viral protein]]

2bsg

From Proteopedia

Current revision

The modeled structure of fibritin (gpwac) of bacteriophage T4 based on cryo-EM reconstruction of the extended tail of bacteriophage T4

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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