View source for 7cpz


==Crystal structure of Streptoavidin-C1 from Streptomyces cinamonensis==
<StructureSection load='7cpz' size='340' side='right'caption='[[7cpz]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cpz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._H036 Streptomyces sp. H036]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CPZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</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=7cpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cpz OCA], [https://pdbe.org/7cpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cpz RCSB], [https://www.ebi.ac.uk/pdbsum/7cpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cpz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M8UVL7_9ACTN A0A0M8UVL7_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The members of the avidin protein family are well known for their high affinity towards d-biotin and their structural stability. These properties make avidins a valuable tool for various biotechnological applications. In the present study, two avidin-like biotin-binding proteins (named streptavidin C1 and C2) from Streptomyces cinnamonensis were newly identified while exploring antifungal proteins against Fusarium oxysporum f. sp. cucumerinum. Streptavidin C1 reveals a low correlation (a sequence identity of approximately 64%) with all known streptavidins, whereas streptavidin C2 shares a sequence identity of approximately 94% with other streptavidins. Here, the crystal structures of streptavidin C1 in the mature form and in complex with biotin at 2.1 and 2.5 A resolution, respectively, were assessed. The overall structures present similar tetrameric features with D 2 symmetry to other (strept)avidin structures. Interestingly, the long C-terminal region comprises a short alpha-helix (C-Lid; residues 169-179) and an extension C-terminal peptide (ECP; residues 180-191) which stretches into the biotin-binding sites of the same monomer. This ECP sequence (-(180)VTSANPPAS(188)-) is a newly defined biotin-binding site, which reduces the ability to bind to (strept)avidin family proteins. The novel streptavidin C1 could help in the development of an engineered tetrameric streptavidin with reduced biotin-binding capacity as well as other biomaterial tools.

Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites.,Jeon BJ, Kim S, Kim MS, Lee JH, Kim BS, Hwang KY IUCrJ. 2021 Jan 11;8(Pt 2):168-177. doi: 10.1107/S2052252520015675. eCollection, 2021 Mar 1. PMID:33708394<ref>PMID:33708394</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cpz" style="background-color:#fffaf0;"></div>

==See Also==
*[[Avidin 3D structures|Avidin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. H036]]
[[Category: Hwang KY]]
[[Category: Jeon BJ]]
[[Category: Kim MS]]
[[Category: Kim S]]
[[Category: Lee J-H]]