6jta: Difference between revisions

Latest revision as of 10:19, 22 November 2023

Crystal Structure of D464A L465A mutant of FGAM Synthetase

Structural highlights

6jta 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.
Method:	X-ray diffraction, Resolution 1.75Å
Ligands:	ADP, EDO, GLN, GOL, MG, SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PUR4_SALTY

Publication Abstract from PubMed

Transient tunnels that assemble and disassemble to facilitate passage of unstable intermediates in enzymes containing multiple reaction centers are controlled by allosteric cues. Using the 140-kDa purine biosynthetic enzyme PurL as a model system and a combination of biochemical and x-ray crystallographic studies, we show that long-distance communication between ~25-A distal active sites is initiated by an allosteric switch, residing in a conserved catalytic loop, adjacent to the synthetase active site. Further, combinatory experiments seeded from molecular dynamics simulations help to delineate transient states that bring out the central role of nonfunctional adaptor domains. We show that carefully orchestrated conformational changes, facilitated by interplay of dynamic interactions at the allosteric switch and adaptor-domain interface, control reactivity and concomitant formation of the ammonia tunnel. This study asserts that substrate channeling is modulated by allosteric hotspots that alter protein energy landscape, thereby allowing the protein to adopt transient conformations paramount to function.

Role of allosteric switches and adaptor domains in long-distance cross-talk and transient tunnel formation.,Sharma N, Ahalawat N, Sandhu P, Strauss E, Mondal J, Anand R Sci Adv. 2020 Apr 3;6(14):eaay7919. doi: 10.1126/sciadv.aay7919. eCollection 2020, Apr. PMID:32284973^[1]

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

References

↑ Sharma N, Ahalawat N, Sandhu P, Strauss E, Mondal J, Anand R. Role of allosteric switches and adaptor domains in long-distance cross-talk and transient tunnel formation. Sci Adv. 2020 Apr 3;6(14):eaay7919. doi: 10.1126/sciadv.aay7919. eCollection 2020, Apr. PMID:32284973 doi:https://dx.doi.org/10.1126/sciadv.aay7919

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OCA

[1] Sharma N, Ahalawat N, Sandhu P, Strauss E, Mondal J, Anand R. Role of allosteric switches and adaptor domains in long-distance cross-talk and transient tunnel formation. Sci Adv. 2020 Apr 3;6(14):eaay7919. doi: 10.1126/sciadv.aay7919. eCollection 2020, Apr. PMID:32284973 doi:https://dx.doi.org/10.1126/sciadv.aay7919

[1]

@@ Line 3: / Line 3: @@
 <StructureSection load='6jta' size='340' side='right'caption='[[6jta]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6jta]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JTA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JTA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6jta]] 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=6JTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JTA 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.75&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">purL, C2273_06610, DD95_10355 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6jta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jta OCA], [https://pdbe.org/6jta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jta RCSB], [https://www.ebi.ac.uk/pdbsum/6jta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jta ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jta OCA], [http://pdbe.org/6jta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jta RCSB], [http://www.ebi.ac.uk/pdbsum/6jta PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jta ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A0A0D6F9Y3_SALTM A0A0D6F9Y3_SALTM]] Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.[HAMAP-Rule:MF_00419][SAAS:SAAS01200885]
+[https://www.uniprot.org/uniprot/PUR4_SALTY PUR4_SALTY]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus typhimurium loeffler 1892]]
 [[Category: Large Structures]]
-[[Category: Phosphoribosylformylglycinamidine synthase]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-[[Category: Ahalawat, N]]
+[[Category: Ahalawat N]]
-[[Category: Anand, R]]
+[[Category: Anand R]]
-[[Category: Mondal, J]]
+[[Category: Mondal J]]
-[[Category: Sandhu, P]]
+[[Category: Sandhu P]]
-[[Category: Sharma, N]]
+[[Category: Sharma N]]
-[[Category: Biosynthetic protein]]
-[[Category: Fgam synthetase]]

6jta: Difference between revisions

Latest revision as of 10:19, 22 November 2023

Crystal Structure of D464A L465A mutant of FGAM Synthetase

Structural highlights

Function

Publication Abstract from PubMed

References

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