View source for 7cay


==Crystal Structure of Lon N-terminal domain protein from Xanthomonas campestris==
<StructureSection load='7cay' size='340' side='right'caption='[[7cay]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cay]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris Xanthomonas campestris pv. campestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CAY 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]] 2.8&#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=7cay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cay OCA], [https://pdbe.org/7cay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cay RCSB], [https://www.ebi.ac.uk/pdbsum/7cay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cay ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8P5P7_XANCP Q8P5P7_XANCP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
LonA peptidase is a major component of the protein quality-control mechanism in both prokaryotes and the organelles of eukaryotes. Proteins homologous to the N-terminal domain of LonA peptidase, but lacking its other domains, are conserved in several phyla of prokaryotes, including the Xanthomonadales order. However, the function of these homologous proteins (LonNTD-like proteins) is not known. Here, the crystal structure of the LonNTD-like protein from Xanthomonas campestris (XCC3289; UniProt Q8P5P7) is reported at 2.8 A resolution. The structure was solved by molecular replacement and contains one polypeptide in the asymmetric unit. The structure was refined to an Rfree of 29%. The structure of XCC3289 consists of two domains joined by a long loop. The N-terminal domain (residues 1-112) consists of an alpha-helix surrounded by beta-sheets, whereas the C-terminal domain (residues 123-193) is an alpha-helical bundle. The fold and spatial orientation of the two domains closely resembles those of the N-terminal domains of the LonA peptidases from Escherichia coli and Mycobacterium avium. The structure is also similar to that of cereblon, a substrate-recognizing component of the E3 ubiquitin ligase complex. The N-terminal domains of both LonA and cereblon are known to be involved in specific protein-protein interactions. This structural analysis suggests that XCC3289 and other LonNTD-like proteins might also be capable of such protein-protein interactions.

Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase.,Singh R, Deshmukh S, Kumar A, Goyal VD, Makde RD Acta Crystallogr F Struct Biol Commun. 2020 Oct 1;76(Pt 10):488-494. doi:, 10.1107/S2053230X20011875. Epub 2020 Sep 16. PMID:33006577<ref>PMID:33006577</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cay" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xanthomonas campestris pv. campestris]]
[[Category: Deshmukh S]]
[[Category: Kumar A]]
[[Category: Makde RD]]
[[Category: Sharma B]]
[[Category: Singh R]]