1vj7

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[[Image:1vj7.gif|left|200px]]<br /><applet load="1vj7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vj7.gif|left|200px]]
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caption="1vj7, resolution 2.10&Aring;" />
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'''Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis.'''<br />
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{{Structure
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|PDB= 1vj7 |SIZE=350|CAPTION= <scene name='initialview01'>1vj7</scene>, resolution 2.10&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> and <scene name='pdbligand=GPX:GUANOSINE 5'-DIPHOSPHATE 2':3'-CYCLIC MONOPHOSPHATE'>GPX</scene>
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|ACTIVITY=
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|GENE= RELA, REL, SPOT, RSH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=119602 Streptococcus dysgalactiae subsp. equisimilis])
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}}
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'''Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1VJ7 is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15066282 15066282]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15066282 15066282]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus dysgalactiae subsp. equisimilis]]
[[Category: Streptococcus dysgalactiae subsp. equisimilis]]
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[[Category: stringent response]]
[[Category: stringent response]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:46:21 2008''

Revision as of 12:46, 20 March 2008

Image:1vj7.gif


PDB ID 1vj7

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: , and
Gene: RELA, REL, SPOT, RSH (Streptococcus dysgalactiae subsp. equisimilis)
Coordinates: save as pdb, mmCIF, xml



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. 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

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