7tdv - Revision history

OCA at 17:03, 18 October 2023

OCA — Wed, 18 Oct 2023 17:03:43 GMT

←Older revision		Revision as of 17:03, 18 October 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7tdv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TDV FirstGlance]. <br>		<table><tr><td colspan='2'>[[7tdv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TDV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.92Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=7tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tdv OCA], [https://pdbe.org/7tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tdv RCSB], [https://www.ebi.ac.uk/pdbsum/7tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tdv 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=7tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tdv OCA], [https://pdbe.org/7tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tdv RCSB], [https://www.ebi.ac.uk/pdbsum/7tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tdv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/E3VXC2_STAAU E3VXC2_STAAU]] Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.[ARBA:ARBA00002161]	+	[https://www.uniprot.org/uniprot/E3VXC2_STAAU E3VXC2_STAAU] Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.[ARBA:ARBA00002161]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 7tdv" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 7tdv" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutamine synthetase 3D structures\|Glutamine synthetase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:25, 8 September 2022

OCA — Thu, 08 Sep 2022 06:25:47 GMT

←Older revision		Revision as of 06:25, 8 September 2022
Line 3:		Line 3:
	<StructureSection load='7tdv' size='340' side='right'caption='[[7tdv]], [[Resolution\|resolution]] 2.92Å' scene=''>		<StructureSection load='7tdv' size='340' side='right'caption='[[7tdv]], [[Resolution\|resolution]] 2.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7tdv]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TDV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7tdv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TDV FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] </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=7tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tdv OCA], [https://pdbe.org/7tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tdv RCSB], [https://www.ebi.ac.uk/pdbsum/7tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tdv 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=7tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tdv OCA], [https://pdbe.org/7tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tdv RCSB], [https://www.ebi.ac.uk/pdbsum/7tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tdv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/E3VXC2_STAAU E3VXC2_STAAU]] Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.[ARBA:ARBA00002161]	+	[[https://www.uniprot.org/uniprot/E3VXC2_STAAU E3VXC2_STAAU]] Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.[ARBA:ARBA00002161]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Glutamate--ammonia ligase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Schumacher, M A~~]]	+	[[Category: Staphylococcus aureus]]
-	[[Category: ~~Femc]]~~	+	[[Category: Schumacher MA]]
-	~~[[Category: Glnr]]~~	+
-	~~[[Category: Glutamate-ammonium ligase]]~~	+
-	~~[[Category: Glutamine synthetase]]~~	+
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: S. aureus~~]]	+

OCA at 05:27, 13 July 2022

OCA — Wed, 13 Jul 2022 05:27:08 GMT

←Older revision		Revision as of 05:27, 13 July 2022
Line 1:		Line 1:

	==Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state complex==		==Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state complex==
-	<StructureSection load='7tdv' size='340' side='right'caption='[[7tdv]]' scene=''>	+	<StructureSection load='7tdv' size='340' side='right'caption='[[7tdv]], [[Resolution\|resolution]] 2.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TDV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7tdv]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TDV FirstGlance]. <br>
-	</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=7tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tdv OCA], [https://pdbe.org/7tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tdv RCSB], [https://www.ebi.ac.uk/pdbsum/7tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tdv ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P3S:L-METHIONINE-S-SULFOXIMINE+PHOSPHATE'>P3S</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] </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=7tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tdv OCA], [https://pdbe.org/7tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tdv RCSB], [https://www.ebi.ac.uk/pdbsum/7tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tdv ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/E3VXC2_STAAU E3VXC2_STAAU]] Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.[ARBA:ARBA00002161]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	How bacteria sense and respond to nitrogen levels are central questions in microbial physiology. In Gram-positive bacteria, nitrogen homeostasis is controlled by an operon encoding glutamine synthetase (GS), a dodecameric machine that assimilates ammonium into glutamine, and the GlnR repressor. GlnR detects nitrogen excess indirectly by binding glutamine-feedback-inhibited-GS (FBI-GS), which activates its transcription-repression function. The molecular mechanisms behind this regulatory circuitry, however, are unknown. Here we describe biochemical and structural analyses of GS and FBI-GS-GlnR complexes from pathogenic and non-pathogenic Gram-positive bacteria. The structures show FBI-GS binds the GlnR C-terminal domain within its active-site cavity, juxtaposing two GlnR monomers to form a DNA-binding-competent GlnR dimer. The FBI-GS-GlnR interaction stabilizes the inactive GS conformation. Strikingly, this interaction also favors a remarkable dodecamer to tetradecamer transition in some GS, breaking the paradigm that all bacterial GS are dodecamers. These data thus unveil unique structural mechanisms of transcription and enzymatic regulation.
		+
		+	Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.,Travis BA, Peck JV, Salinas R, Dopkins B, Lent N, Nguyen VD, Borgnia MJ, Brennan RG, Schumacher MA Nat Commun. 2022 Jul 1;13(1):3793. doi: 10.1038/s41467-022-31573-0. PMID:35778410<ref>PMID:35778410</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7tdv" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Glutamate--ammonia ligase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Schumacher, MA]]	+	[[Category: Schumacher, M A]]
		+	[[Category: Femc]]
		+	[[Category: Glnr]]
		+	[[Category: Glutamate-ammonium ligase]]
		+	[[Category: Glutamine synthetase]]
		+	[[Category: Ligase]]
		+	[[Category: S. aureus]]

OCA at 07:27, 29 June 2022

OCA — Wed, 29 Jun 2022 07:27:29 GMT

←Older revision		Revision as of 07:27, 29 June 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 7tdv is ON HOLD until Paper Publication~~	+	==Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state complex==
-		+	<StructureSection load='7tdv' size='340' side='right'caption='[[7tdv]]' scene=''>
-	~~Authors: Schumacher, M.A.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TDV FirstGlance]. <br>
-	~~Description:~~ Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state complex	+	</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=7tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tdv OCA], [https://pdbe.org/7tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tdv RCSB], [https://www.ebi.ac.uk/pdbsum/7tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tdv ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Schumacher, ~~M.A~~]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Schumacher, MA]]

OCA at 06:16, 9 February 2022

OCA — Wed, 09 Feb 2022 06:16:39 GMT

←Older revision		Revision as of 06:16, 9 February 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7tdv is ON HOLD	+	The entry 7tdv is ON HOLD until Paper Publication

	Authors: Schumacher, M.A.		Authors: Schumacher, M.A.

OCA: Protected "7tdv" [edit=sysop:move=sysop]

OCA — Wed, 12 Jan 2022 08:37:44 GMT

Protected "7tdv" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:37, 12 January 2022

OCA: New page: '''Unreleased structure''' The entry 7tdv is ON HOLD Authors: Schumacher, M.A. Description: Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state comple...

OCA — Wed, 12 Jan 2022 08:37:43 GMT

New page: '''Unreleased structure''' The entry 7tdv is ON HOLD Authors: Schumacher, M.A. Description: Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state comple...

New page

'''Unreleased structure'''

The entry 7tdv is ON HOLD

Authors: Schumacher, M.A.

Description: Crystal structure of S. aureus glutamine synthetase in Met-Sox-P/ADP transition state complex
[[Category: Unreleased Structures]]
[[Category: Schumacher, M.A]]