3kxi

<StructureSection load='3kxi' size='340' side='right' caption='[[3kxi]], [[Resolution|resolution]] 2.65&Aring;' scene=''>

<table><tr><td colspan='2'>[[3kxi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KXI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KXI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qth|2qth]], [[3kxk|3kxk]], [[3kxl|3kxl]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hflX, SSO0269 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kxi OCA], [http://pdbe.org/3kxi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kxi RCSB], [http://www.ebi.ac.uk/pdbsum/3kxi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kxi ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/HFLX_SULSO HFLX_SULSO]] GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. Specific for GTP.[HAMAP-Rule:MF_00900]<ref>PMID:19787775</ref> <ref>PMID:21478358</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kx/3kxi_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

GTPase domains from members of the HflX protein family have their catalytic glutamine residue of the DxxGQ motif substituted by phenylalanine, while they are still able to hydrolyse GTP. This appears to challenge the traditional view of GTP hydrolysis mechanism of Ras-like GTPases. SsGBP from the hyperthermophilic archaeon Sulfolobus solfataricus provided the first crystal structure of the HflX family. Here, we report structure-based mutagenesis analyses on SsGBP. Six-point mutations were individually introduced in the Ras-like GTPase domain including regions of P-loop, switches I and II. Intrinsic GTPase activities and thermal stabilities of these variants together with the wild-type full-length SsGBP and its isolated GTPase domain were analysed. Both functional and structural analyses of G235P and G235S mutants, which showed total and partial loss of the GTP hydrolyzing activity, respectively, support our hypothesis that the role of aligning a nucleophilic water molecule by the Ras Gln60 residue is replaced by the backbone amide group of Gly235 in SsGBP. Together with functional studies of other mutants, we conclude that the classical view of GTP hydrolysis mechanism likely remains the same in the HflX family with a twist in the entity of the nucleophilic alignment.

Functional study on GTP hydrolysis by the GTP-binding protein from Sulfolobus solfataricus, a member of the HflX family.,Huang B, Wu H, Hao N, Blombach F, van der Oost J, Li X, Zhang XC, Rao Z J Biochem. 2010 Jul;148(1):103-13. Epub 2010 Apr 16. PMID:20400571<ref>PMID:20400571</ref>

 

[[Category: Atcc 35091]]

[[Category: Huang, B]]

[[Category: Li, X]]

[[Category: Rao, Z]]

[[Category: Zhang, X C]]

[[Category: Gtp-binding]]

[[Category: Gtpase]]

[[Category: Ssgbp]]