This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3ugj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:38, 20 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Formyl Glycinamide ribonucletide amidotransferase from Salmonella Typhimurum: Role of the ATP complexation and glutaminase domain in catalytic coupling==
==Formyl Glycinamide ribonucletide amidotransferase from Salmonella Typhimurum: Role of the ATP complexation and glutaminase domain in catalytic coupling==
-
<StructureSection load='3ugj' size='340' side='right' caption='[[3ugj]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
+
<StructureSection load='3ugj' size='340' side='right'caption='[[3ugj]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3ugj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium Salmonella enterica subsp. enterica serovar typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UGJ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3ugj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UGJ FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.78&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t3t|1t3t]]</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoribosylformylglycinamidine_synthase Phosphoribosylformylglycinamidine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.3 6.3.5.3] </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=3ugj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ugj OCA], [https://pdbe.org/3ugj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ugj RCSB], [https://www.ebi.ac.uk/pdbsum/3ugj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ugj ProSAT]</span></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=3ugj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ugj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ugj RCSB], [http://www.ebi.ac.uk/pdbsum/3ugj PDBsum]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/PUR4_SALTY PUR4_SALTY]
-
Formylglycinamide ribonucleotide (FGAR) amidotransferase (FGAR-AT) takes part in purine biosynthesis and is a multidomain enzyme with multiple spatially separated active sites. FGAR-AT contains a glutaminase domain that is responsible for the generation of ammonia from glutamine. Ammonia is then transferred via a channel to a second active site located in the synthetase domain and utilized to convert FGAR to formylglycinamidine ribonucleotide (FGAM) in an adenosine triphosphate (ATP) dependent reaction. In some ammonia-channelling enzymes ligand binding triggers interdomain signalling between the two diverse active centres and also assists in formation of the ammonia channel. Previously, the structure of FGAR-AT from Salmonella typhimurium containing a glutamyl thioester intermediate covalently bound in the glutaminase active site was determined. In this work, the roles played by various ligands of FGAR-AT in inducing catalytic coupling are investigated. Structures of FGAR-AT from S. typhimurium were determined in two different states: the unliganded form and the binary complex with an ATP analogue in the presence of the glutamyl thioester intermediate. The structures were compared in order to decipher the roles of these two states in interdomain communication. Using a process of elimination, the results indicated that binding of FGAR is most likely to be the major mechanism by which catalytic coupling occurs. This is because conformational changes do not occur either upon formation of the glutamyl thioester intermediate or upon subsequent ATP complexation. A model of the FGAR-bound form of the enzyme suggested that the loop in the synthetase domain may be responsible for initiating catalytic coupling via its interaction with the N-terminal domain.
+
-
 
+
-
Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: role of ATP complexation and the glutaminase domain in catalytic coupling.,Tanwar AS, Morar M, Panjikar S, Anand R Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):627-36. doi:, 10.1107/S0907444912006543. Epub 2012 May 17. PMID:22683785<ref>PMID:22683785</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Phosphoribosylformylglycinamidine synthase]]
+
[[Category: Large Structures]]
-
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
+
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-
[[Category: Anand, R]]
+
[[Category: Anand R]]
-
[[Category: Morar, M]]
+
[[Category: Morar M]]
-
[[Category: Panjikar, S]]
+
[[Category: Panjikar S]]
-
[[Category: Tanwar, A S]]
+
[[Category: Tanwar AS]]
-
[[Category: Amidotransferase]]
+
-
[[Category: Glutaminase]]
+
-
[[Category: Ligase]]
+
-
[[Category: Thioester intermediate]]
+

Current revision

Formyl Glycinamide ribonucletide amidotransferase from Salmonella Typhimurum: Role of the ATP complexation and glutaminase domain in catalytic coupling

PDB ID 3ugj

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ugj"
Personal tools