View source for 4y6c


==Q17M crystal structure of Podosopora anserina putative kinesin light chain nearly identical TPR-like repeats==
<StructureSection load='4y6c' size='340' side='right'caption='[[4y6c]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4y6c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y6C FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4y6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y6c OCA], [https://pdbe.org/4y6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y6c RCSB], [https://www.ebi.ac.uk/pdbsum/4y6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y6c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A090CRQ5_PODAN A0A090CRQ5_PODAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Linear repeat proteins often have high structural similarity and low ( approximately 25%) pairwise sequence identities (PSI) among modules. We identified a unique P. anserina (Pa) sequence with tetratricopeptide repeat (TPR) homology, which contains longer (42 residue) repeats (42PRs) with an average PSI &gt;91%. We determined the crystal structure of five tandem Pa 42PRs to 1.6 A, and examined the stability and solution properties of constructs containing three to six Pa 42PRs. Compared with 34-residue TPRs (34PRs), Pa 42PRs have a one-turn extension of each helix, and bury more surface area. Unfolding transitions shift to higher denaturant concentration and become sharper as repeats are added. Fitted Ising models show Pa 42PRs to be more cooperative than consensus 34PRs, with increased magnitudes of intrinsic and interfacial free energies. These results demonstrate the tolerance of the TPR motif to length variation, and provide a basis to understand the effects of helix length on intrinsic/interfacial stability.

A Naturally Occurring Repeat Protein with High Internal Sequence Identity Defines a New Class of TPR-like Proteins.,Marold JD, Kavran JM, Bowman GD, Barrick D Structure. 2015 Oct 1. pii: S0969-2126(15)00369-X. doi:, 10.1016/j.str.2015.07.022. PMID:26439765<ref>PMID:26439765</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4y6c" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Podospora anserina]]
[[Category: Barrick D]]
[[Category: Bowman GD]]
[[Category: Kavran JM]]
[[Category: Marold JD]]