This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4dwl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 2: Line 2:
<StructureSection load='4dwl' size='340' side='right' caption='[[4dwl]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
<StructureSection load='4dwl' size='340' side='right' caption='[[4dwl]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4dwl]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bordetella_phage_bpp-1 Bordetella phage bpp-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DWL FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4dwl]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpbpp Bpbpp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DWL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bbp7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=194699 Bordetella phage BPP-1])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bbp7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=194699 BPBPP])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dwl RCSB], [http://www.ebi.ac.uk/pdbsum/4dwl PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dwl RCSB], [http://www.ebi.ac.uk/pdbsum/4dwl PDBsum]</span></td></tr>
</table>
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Diversity-generating retroelements (DGRs) are the only known source of massive protein sequence variation in prokaryotes. These elements transfer coding information from a template region (TR) through an RNA intermediate to a protein-encoding variable region. This retrohoming process is accompanied by unique adenine-specific mutagenesis and, in the prototypical BPP-1 DGR, requires a reverse transcriptase (bRT) and an accessory variability determinant (bAvd) protein. To understand the role of bAvd, we determined its 2.69 A resolution structure, which revealed a highly positively charged pentameric barrel. In accordance with its charge, bAvd bound both DNA and RNA, albeit without a discernable sequence preference. We found that the coding sequence of bAvd functioned as part of TR but identified means to mutate bAvd without affecting TR. This mutational analysis revealed a strict correspondence between retrohoming and interaction of bAvd with bRT, suggesting that the bRT-bAvd complex is important for DGR retrohoming.
 +
 +
Structure of the essential diversity-generating retroelement protein bAvd and its functionally important interaction with reverse transcriptase.,Alayyoubi M, Guo H, Dey S, Golnazarian T, Brooks GA, Rong A, Miller JF, Ghosh P Structure. 2013 Feb 5;21(2):266-76. doi: 10.1016/j.str.2012.11.016. Epub 2012 Dec, 27. PMID:23273427<ref>PMID:23273427</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bordetella phage bpp-1]]
+
[[Category: Bpbpp]]
[[Category: Al-Ayyoubi, M]]
[[Category: Al-Ayyoubi, M]]
[[Category: Ghosh, P]]
[[Category: Ghosh, P]]

Revision as of 08:03, 14 January 2015

Avd molecule from Bordetella bacteriophage DGR

4dwl, resolution 2.69Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools