3gqh

<StructureSection load='3gqh' size='340' side='right' caption='[[3gqh]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[3gqh]] is a 3 chain structure with 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=3GQH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GQH FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gq7|3gq7]], [[3gq8|3gq8]], [[3gq9|3gq9]], [[3gqa|3gqa]], [[3gqk|3gqk]], [[3gqn|3gqn]]</td></tr>

<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">12, gene product 12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 Bacillus phage phi29])</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gqh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gqh RCSB], [http://www.ebi.ac.uk/pdbsum/3gqh PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gq/3gqh_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<div style="background-color:#fffaf0;">

== 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<ref>PMID:19450535</ref>

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

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[[Category: Bacillus phage phi29]]

[[Category: Rossmann, M G.]]

[[Category: Xiang, Y.]]

[[Category: Beta barrel]]

[[Category: Viral protein]]