View source for 7zk1


==Crystal structure of cystinosin from Arabidopsis thaliana bound to sybody and nanobody==
<StructureSection load='7zk1' size='340' side='right'caption='[[7zk1]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7zk1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana], [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZK1 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]] 2.65&#8491;</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=7zk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zk1 OCA], [https://pdbe.org/7zk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zk1 RCSB], [https://www.ebi.ac.uk/pdbsum/7zk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zk1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CTNS_ARATH CTNS_ARATH] Thought to transport cystine out of lysosomes.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Amino acid transporters play a key role controlling the flow of nutrients across the lysosomal membrane and regulating metabolism in the cell. Mutations in the gene encoding the transporter cystinosin result in cystinosis, an autosomal recessive metabolic disorder characterised by the accumulation of cystine crystals in the lysosome. Cystinosin is a member of the PQ-loop family of solute carrier (SLC) transporters and uses the proton gradient to drive cystine export into the cytoplasm. However, the molecular basis for cystinosin function remains elusive, hampering efforts to develop novel treatments for cystinosis and understand the mechanisms of ion driven transport in the PQ-loop family. To address these questions, we present the crystal structures of cystinosin from Arabidopsis thaliana in both apo and cystine bound states. Using a combination of in vitro and in vivo based assays, we establish a mechanism for cystine recognition and proton coupled transport. Mutational mapping and functional characterisation of human cystinosin further provide a framework for understanding the molecular impact of disease-causing mutations.

Structural basis for proton coupled cystine transport by cystinosin.,Lobel M, Salphati SP, El Omari K, Wagner A, Tucker SJ, Parker JL, Newstead S Nat Commun. 2022 Aug 17;13(1):4845. doi: 10.1038/s41467-022-32589-2. PMID:35977944<ref>PMID:35977944</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7zk1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Lama glama]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Loebel M]]
[[Category: Newstead S]]
[[Category: Omari KE]]