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3ujn

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Revision as of 20:28, 5 August 2016

Formyl Glycinamide Ribonucleotide Amidotransferase from Salmonella Typhimurium : Role of the ATP complexation and glutaminase domain in catalytic coupling

Structural highlights

3ujn is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	1t3t
Activity:	Phosphoribosylformylglycinamidine synthase, with EC number 6.3.5.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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^[1]

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

References

↑ Tanwar AS, Morar M, Panjikar S, Anand R. Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: role of ATP complexation and the glutaminase domain in catalytic coupling. Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):627-36. doi:, 10.1107/S0907444912006543. Epub 2012 May 17. PMID:22683785 doi:10.1107/S0907444912006543

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ujn"

@@ Line 1: / Line 1: @@
 ==Formyl Glycinamide Ribonucleotide Amidotransferase from Salmonella Typhimurium : Role of the ATP complexation and glutaminase domain in catalytic coupling==
 <StructureSection load='3ujn' size='340' side='right' caption='[[3ujn]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t3t|1t3t]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ujn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ujn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ujn RCSB], [http://www.ebi.ac.uk/pdbsum/3ujn PDBsum]</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=3ujn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ujn OCA], [http://pdbe.org/3ujn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ujn RCSB], [http://www.ebi.ac.uk/pdbsum/3ujn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ujn ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3ujn" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3ujn

From Proteopedia

Revision as of 20:28, 5 August 2016

Formyl Glycinamide Ribonucleotide Amidotransferase from Salmonella Typhimurium : Role of the ATP complexation and glutaminase domain in catalytic coupling

Structural highlights

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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