View source for 6c2v


==Solution structure of a phosphate-loop protein==
<StructureSection load='6c2v' size='340' side='right'caption='[[6c2v]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6c2v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C2V FirstGlance]. <br>
</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=6c2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c2v OCA], [https://pdbe.org/6c2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c2v RCSB], [https://www.ebi.ac.uk/pdbsum/6c2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c2v ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Abundant and essential motifs, such as phosphate-binding loops (P-loops), are presumed to be the seeds of modern enzymes. The Walker-A P-loop is absolutely essential in modern NTPase enzymes, in mediating binding, and transfer of the terminal phosphate groups of NTPs. However, NTPase function depends on many additional active-site residues placed throughout the protein's scaffold. Can motifs such as P-loops confer function in a simpler context? We applied a phylogenetic analysis that yielded a sequence logo of the putative ancestral Walker-A P-loop element: a beta-strand connected to an alpha-helix via the P-loop. Computational design incorporated this element into de novo designed beta-alpha repeat proteins with relatively few sequence modifications. We obtained soluble, stable proteins that unlike modern P-loop NTPases bound ATP in a magnesium-independent manner. Foremost, these simple P-loop proteins avidly bound polynucleotides, RNA, and single-strand DNA, and mutations in the P-loop's key residues abolished binding. Binding appears to be facilitated by the structural plasticity of these proteins, including quaternary structure polymorphism that promotes a combined action of multiple P-loops. Accordingly, oligomerization enabled a 55-aa protein carrying a single P-loop to confer avid polynucleotide binding. Overall, our results show that the P-loop Walker-A motif can be implemented in small and simple beta-alpha repeat proteins, primarily as a polynucleotide binding motif.

Simple yet functional phosphate-loop proteins.,Romero Romero ML, Yang F, Lin YR, Toth-Petroczy A, Berezovsky IN, Goncearenco A, Yang W, Wellner A, Kumar-Deshmukh F, Sharon M, Baker D, Varani G, Tawfik DS Proc Natl Acad Sci U S A. 2018 Nov 30. pii: 1812400115. doi:, 10.1073/pnas.1812400115. PMID:30504143<ref>PMID:30504143</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6c2v" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Baker D]]
[[Category: Lin YR]]
[[Category: Romero Romero ML]]
[[Category: Tawfik D]]
[[Category: Varani G]]
[[Category: Yang F]]
[[Category: Yang W]]