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| | <StructureSection load='6jt8' size='340' side='right'caption='[[6jt8]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='6jt8' size='340' side='right'caption='[[6jt8]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jt8]] 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=6JT8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JT8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jt8]] 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=6JT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JT8 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=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]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYG:2-AMINO-4-(AMINO-3-OXO-PROPYLSULFANYLCARBONYL)-BUTYRIC+ACID'>CYG</scene></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=CYG:2-AMINO-4-(AMINO-3-OXO-PROPYLSULFANYLCARBONYL)-BUTYRIC+ACID'>CYG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jt8 OCA], [https://pdbe.org/6jt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jt8 RCSB], [https://www.ebi.ac.uk/pdbsum/6jt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jt8 ProSAT]</span></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://proteopedia.org/fgij/fg.htm?mol=6jt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jt8 OCA], [http://pdbe.org/6jt8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jt8 RCSB], [http://www.ebi.ac.uk/pdbsum/6jt8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jt8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus typhimurium loeffler 1892]] | |
| | [[Category: Large Structures]] | | [[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]]
| + | |
| Structural highlights
6jt8 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 1.9Å |
| Ligands: | , , , , , |
| 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:http://dx.doi.org/10.1126/sciadv.aay7919
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