View source for 4phg


==Crystal structure of Ypt7 covalently modified with GTP==
<StructureSection load='4phg' size='340' side='right'caption='[[4phg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4phg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PHG 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2UJ:N-[3-(PROPANOYLAMINO)PROPYL]GUANOSINE+5-(TETRAHYDROGEN+TRIPHOSPHATE)'>2UJ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</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=4phg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4phg OCA], [https://pdbe.org/4phg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4phg RCSB], [https://www.ebi.ac.uk/pdbsum/4phg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4phg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YPT7_YEAST YPT7_YEAST] Needed for homotypic vacuole fusion, the last step in the vacuole inheritance process.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GTPases act as key regulators of many cellular processes by switching between active (GTP-bound) and inactive (GDP-bound) states. In many cases, understanding their mode of action has been aided by artificially stabilizing one of these states either by designing mutant proteins or by complexation with non-hydrolysable GTP analogues. Because of inherent disadvantages in these approaches, we have developed acryl-bearing GTP and GDP derivatives that can be covalently linked with strategically placed cysteines within the GTPase of interest. Binding studies with GTPase-interacting proteins and X-ray crystallography analysis demonstrate that the molecular properties of the covalent GTPase-acryl-nucleotide adducts are a faithful reflection of those of the corresponding native states and are advantageously permanently locked in a defined nucleotide (that is active or inactive) state. In a first application, in vivo experiments using covalently locked Rab5 variants provide new insights into the mechanism of correct intracellular localization of Rab proteins.

Locking GTPases covalently in their functional states.,Wiegandt D, Vieweg S, Hofmann F, Koch D, Li F, Wu YW, Itzen A, Muller MP, Goody RS Nat Commun. 2015 Jul 16;6:7773. doi: 10.1038/ncomms8773. PMID:26178622<ref>PMID:26178622</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4phg" style="background-color:#fffaf0;"></div>

==See Also==
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Goody RS]]
[[Category: Hofmann F]]
[[Category: Itzen A]]
[[Category: Koch D]]
[[Category: Mueller MP]]
[[Category: Vieweg S]]
[[Category: Wiegandt D]]
[[Category: Wu Y]]