View source for 9jju


==Truncated RNF112, nucleotide-free==
<StructureSection load='9jju' size='340' side='right'caption='[[9jju]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jju]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9JJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JJU 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]] 2.09&#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=9jju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jju OCA], [https://pdbe.org/9jju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jju RCSB], [https://www.ebi.ac.uk/pdbsum/9jju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jju ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2VPQ0_XENLA Q2VPQ0_XENLA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Most members of the dynamin superfamily of large guanosine triphophatases (GTPases) have an ability to remodel membranes in response to guanosine triphosphate (GTP) hydrolysis. Ring Finger Protein 112 (RNF112) (ZNF179/neurolastin) is a recently identified brain-specific dynamin-like protein possessing a really interesting new gene (RING) finger domain. Despite its essential role as an E3 ligase in neuron development, the architecture of RNF112 and the exact role of its GTPase activity remain unknown. Here, we determined the crystal structure of truncated RNF112 (RNF112(T)) containing a GTPase domain (GD) and three-helical middle domain (MD) at different nucleotide-loading states. In the nucleotide-free (apo) state, the monomeric RNF112(T) remained in a unique self-restraint conformation characterized by docking of the proximal end of the MD to a groove in the GD. At the transition state of GTP hydrolysis, the MD was released from the GD and stretched aside to form an intertwined RNF112(T) homodimer. Engineered RNF112 equipped with the C-terminal elements of ATL1 or the two transmembrane domains of yeast Sac1p relocated to the endoplasmic reticulum and was capable of mediating membrane remodeling. Taken together, our results offer necessary understandings of RNF112 as a dynamin-like large GTPase in its cellular function and provide insights into the functional mechanisms of dynamin superfamily proteins.

Structural and functional characterization of the brain-specific dynamin superfamily member RNF112.,Zhong YT, Huang LL, Li K, Yang B, Ye X, Zhong HR, Yu B, Ma M, Yuan Y, Meng Y, Pan R, Zhang H, Shi L, Wang Y, Tian R, Gao S, Bian X Proc Natl Acad Sci U S A. 2025 Apr 15;122(15):e2419449122. doi: , 10.1073/pnas.2419449122. Epub 2025 Apr 8. PMID:40198702<ref>PMID:40198702</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9jju" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Gao S]]
[[Category: Huang LL]]
[[Category: Zhong YT]]