1vj7

From Proteopedia

(Difference between revisions)

Revision as of 07:37, 30 December 2020

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

Structural highlights

1vj7 is a 2 chain structure with sequence from "streptococcus_equisimilis"_frost_and_engelbrecht_1936_(human_strains) "streptococcus equisimilis" frost and engelbrecht 1936 (human strains). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	RELA, REL, SPOT, RSH ("Streptococcus equisimilis" Frost and Engelbrecht 1936 (human strains))
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hogg T, Mechold U, Malke H, Cashel M, Hilgenfeld R. Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response [corrected]. Cell. 2004 Apr 2;117(1):57-68. PMID:15066282

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vj7"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis.==
-<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 ==
-<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VJ7 FirstGlance]. <br>
+<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>
-</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=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='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='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='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=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'>[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>
 </table>
 == Function ==
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Cashel, M]]
 [[Category: Hilgenfeld, R]]

1vj7

From Proteopedia

Revision as of 07:37, 30 December 2020

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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