1vj7
From Proteopedia
(New page: 200px<br /><applet load="1vj7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vj7, resolution 2.10Å" /> '''Crystal structure of...) |
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| - | [[Image:1vj7.gif|left|200px]]<br /><applet load="1vj7" size=" | + | [[Image:1vj7.gif|left|200px]]<br /><applet load="1vj7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vj7, resolution 2.10Å" /> | caption="1vj7, resolution 2.10Å" /> | ||
'''Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis.'''<br /> | '''Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1VJ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_dysgalactiae_subsp._equisimilis Streptococcus dysgalactiae subsp. equisimilis] with MN, GDP and GPX as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1VJ7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_dysgalactiae_subsp._equisimilis Streptococcus dysgalactiae subsp. equisimilis] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=GPX:'>GPX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJ7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: stringent response]] | [[Category: stringent response]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:00 2008'' |
Revision as of 13:36, 21 February 2008
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Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis.
Overview
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.
About this Structure
1VJ7 is a Single protein structure of sequence from Streptococcus dysgalactiae subsp. equisimilis with , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:36:00 2008
Categories: Single protein | Streptococcus dysgalactiae subsp. equisimilis | Cashel, M. | Hilgenfeld, R. | Hogg, T. | Malke, H. | Mechold, U. | GDP | GPX | MN | (p)ppgpp | Alpha beta 2-layer sandwich | Gdp | Hd domain | Helix bundle | Magic spot | Manganese | Ppg2':3'p | Ppgpp | Rela | Rsh | Spot | Stringent effector | Stringent factor | Stringent response
