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<StructureSection load='1vj7' size='340' side='right'caption='[[1vj7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1vj7' size='340' side='right'caption='[[1vj7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1vj7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptococcus_equisimilis"_frost_and_engelbrecht_1936_(human_strains) "streptococcus equisimilis" frost and engelbrecht 1936 (human strains)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJ7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1VJ7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1vj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_dysgalactiae_subsp._equisimilis Streptococcus dysgalactiae subsp. equisimilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VJ7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GPX:GUANOSINE+5-DIPHOSPHATE+2 3-CYCLIC+MONOPHOSPHATE'>GPX</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RELA, REL, SPOT, RSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119602 "Streptococcus equisimilis" Frost and Engelbrecht 1936 (human strains)])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GPX:GUANOSINE+5-DIPHOSPHATE+2 3-CYCLIC+MONOPHOSPHATE'>GPX</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1vj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vj7 OCA], [http://pdbe.org/1vj7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vj7 RCSB], [http://www.ebi.ac.uk/pdbsum/1vj7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vj7 ProSAT]</span></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=1vj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vj7 OCA], [https://pdbe.org/1vj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vj7 RCSB], [https://www.ebi.ac.uk/pdbsum/1vj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vj7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RELA_STREQ RELA_STREQ]] In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the formation of pppGpp which is then hydrolyzed to form ppGpp, and the hydrolysis of ppGpp. The enzyme does not similtaneously display both synthase and hydrolase activities. In the structure of residues 1-385 there are 2 conformations seen, the hydrolase-OFF/synthase-ON and hydrolase-ON/synthase-OFF, suggesting there is ligand-induced signal transmission between the 2 active sites.  
[https://www.uniprot.org/uniprot/RELA_STREQ RELA_STREQ] In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes both the formation of pppGpp which is then hydrolyzed to form ppGpp, and the hydrolysis of ppGpp. The enzyme does not similtaneously display both synthase and hydrolase activities. In the structure of residues 1-385 there are 2 conformations seen, the hydrolase-OFF/synthase-ON and hydrolase-ON/synthase-OFF, suggesting there is ligand-induced signal transmission between the 2 active sites.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vj7 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vj7 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by producing an intracellular signaling alarmone, (p)ppGpp, which triggers the so-called stringent response. Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. The 2.1 A crystal structure of the bifunctional catalytic fragment of the Rel/Spo homolog from Streptococcus dysgalactiae subsp. equisimilis, Rel(Seq), reveals two conformations of the enzyme corresponding to known reciprocal activity states: (p)ppGpp-hydrolase-OFF/(p)ppGpp-synthetase-ON and hydrolase-ON/synthetase-OFF. The hydrolase and synthetase domains bear remarkable similarities to the catalytic domains of the cyclic phosphodiesterase and nucleotidyltransferase superfamilies, respectively. The active sites, separated by more than 30 A, contain bound nucleotides including an unusual (p)ppGpp derivative, GDP-2':3'-cyclic monophosphate. Reciprocal regulation of the antagonistic catalytic activities, suggested by the structure, is supported by mutagenesis experiments and appears to involve ligand-induced signal transmission between the two active sites.
Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response [corrected].,Hogg T, Mechold U, Malke H, Cashel M, Hilgenfeld R Cell. 2004 Apr 2;117(1):57-68. PMID:15066282<ref>PMID:15066282</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1vj7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cashel, M]]
[[Category: Streptococcus dysgalactiae subsp. equisimilis]]
[[Category: Hilgenfeld, R]]
[[Category: Cashel M]]
[[Category: Hogg, T]]
[[Category: Hilgenfeld R]]
[[Category: Malke, H]]
[[Category: Hogg T]]
[[Category: Mechold, U]]
[[Category: Malke H]]
[[Category: Alpha beta 2-layer sandwich]]
[[Category: Mechold U]]
[[Category: Gdp]]
[[Category: Hd domain]]
[[Category: Helix bundle]]
[[Category: Hydrolase]]
[[Category: Magic spot]]
[[Category: Manganese]]
[[Category: Ppg2':3'p]]
[[Category: Ppgpp]]
[[Category: Rela]]
[[Category: Rsh]]
[[Category: Spot]]
[[Category: Stringent effector]]
[[Category: Stringent factor]]
[[Category: Stringent response]]
[[Category: Transferase]]

Latest revision as of 08:46, 14 February 2024

Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis.

1vj7, resolution 2.10Å

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