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3gqa

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Crystal Structure of the Bacteriophage phi29 gene product 12 N-terminal fragment in complex with cobalt ions

Structural highlights

3gqa is a 1 chain structure with sequence from Bacillus virus phi29. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FIB12_BPPH2 Structural component of the 12 appendages that hang from the lower collar. Adhesion protein that binds to the host cell surface during virus attachment and mediates teichoic acids degradation.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The tailed bacteriophage phi29 has 12 "appendages" (gene product 12, gp12) attached to its neck region that participate in host cell recognition and entry. In the cell, monomeric gp12 undergoes proteolytic processing that releases the C-terminal domain during assembly into trimers. We report here crystal structures of the protein before and after catalytic processing and show that the C-terminal domain of gp12 is an "autochaperone" that aids trimerization. We also show that autocleavage of the C-terminal domain is a posttrimerization event that is followed by a unique ATP-dependent release. The posttranslationally modified N-terminal part has three domains that function to attach the appendages to the phage, digest the cell wall teichoic acids, and bind irreversibly to the host, respectively. Structural and sequence comparisons suggest that some eukaryotic and bacterial viruses as well as bacterial adhesins might have a similar maturation mechanism as is performed by phi29 gp12 for Bacillus subtilis.

Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike.,Xiang Y, Leiman PG, Li L, Grimes S, Anderson DL, Rossmann MG Mol Cell. 2009 May 15;34(3):375-86. PMID:19450535^[2]

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

References

↑ Villanueva N, Salas M. Adsorption of bacteriophage phi 29 to Bacillus subtilis through the neck appendages of the viral particle. J Virol. 1981 Apr;38(1):15-9. PMID:7241648
↑ Xiang Y, Leiman PG, Li L, Grimes S, Anderson DL, Rossmann MG. Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike. Mol Cell. 2009 May 15;34(3):375-86. PMID:19450535 doi:10.1016/j.molcel.2009.04.009

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3gqa"

Categories: Bacillus virus phi29 | Large Structures | Rossmann MG | Xiang Y

@@ Line 3: / Line 3: @@
 <StructureSection load='3gqa' size='340' side='right'caption='[[3gqa]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3gqa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GQA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3gqa]] is a 1 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=3GQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GQA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gq7|3gq7]], [[3gq8|3gq8]], [[3gq9|3gq9]], [[3gqh|3gqh]], [[3gqk|3gqk]], [[3gqn|3gqn]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">12, gene product 12 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</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=3gqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gqa OCA], [https://pdbe.org/3gqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gqa RCSB], [https://www.ebi.ac.uk/pdbsum/3gqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gqa ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/FIB12_BPPH2 FIB12_BPPH2] Structural component of the 12 appendages that hang from the lower collar. Adhesion protein that binds to the host cell surface during virus attachment and mediates teichoic acids degradation.<ref>PMID:7241648</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Bpph2]]
+[[Category: Bacillus virus phi29]]
 [[Category: Large Structures]]
-[[Category: Rossmann, M G]]
+[[Category: Rossmann MG]]
-[[Category: Xiang, Y]]
+[[Category: Xiang Y]]
-[[Category: Beta helix]]
-[[Category: Viral protein]]

3gqa

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Current revision

Crystal Structure of the Bacteriophage phi29 gene product 12 N-terminal fragment in complex with cobalt ions

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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