4phh: Difference between revisions
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==Crystal structure of Ypt7 covalently modified with GNP== | |||
<StructureSection load='4phh' size='340' side='right'caption='[[4phh]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4phh]] is a 4 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=4PHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PHH 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]] 2.35Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2UK:5-O-[(R)-HYDROXY{[(S)-HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}PHOSPHORYL]-N-[3-(PROPANOYLAMINO)PROPYL]GUANOSINE'>2UK</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4phh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4phh OCA], [https://pdbe.org/4phh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4phh RCSB], [https://www.ebi.ac.uk/pdbsum/4phh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4phh 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4phh" 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]] | |||