5n2p
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Sulfolobus solfataricus Tryptophan Synthase A== | ==Sulfolobus solfataricus Tryptophan Synthase A== | ||
| - | <StructureSection load='5n2p' size='340' side='right' caption='[[5n2p]], [[Resolution|resolution]] 2.06Å' scene=''> | + | <StructureSection load='5n2p' size='340' side='right'caption='[[5n2p]], [[Resolution|resolution]] 2.06Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5n2p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N2P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5n2p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N2P FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpA, SSO0889 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </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=5n2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n2p OCA], [http://pdbe.org/5n2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n2p RCSB], [http://www.ebi.ac.uk/pdbsum/5n2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n2p 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=5n2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n2p OCA], [http://pdbe.org/5n2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n2p RCSB], [http://www.ebi.ac.uk/pdbsum/5n2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n2p ProSAT]</span></td></tr> | ||
| Line 10: | Line 11: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TRPA_SULSO TRPA_SULSO]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.[HAMAP-Rule:MF_00131] | [[http://www.uniprot.org/uniprot/TRPA_SULSO TRPA_SULSO]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.[HAMAP-Rule:MF_00131] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tryptophan synthase (TrpS) is a heterotetrameric alphabetabetaalpha enzyme that exhibits complex substrate channeling and allosteric mechanisms and is a model system in enzymology. In this work, we characterize proposed early and late evolutionary states of TrpS and show that they have distinct quaternary structures, caused by insertions-deletions of sequence segments (indels) in the beta-subunit. Remarkably, indole hydrophobic channels that connect alpha and beta active sites have re-emerged in both TrpS types, yet they follow different paths through the beta-subunit fold. Also, both TrpS geometries activate the alpha-subunit through the rearrangement of loops flanking the active site. Our results link evolutionary sequence changes in the enzyme subunits with channeling and allostery in the TrpS enzymes. The findings demonstrate that indels allow protein quaternary architectures to scape "minima" in the evolutionary landscape, thereby overcoming the conservational constraints imposed by existing functional interfaces and being free to morph into new mechanistic enzymes. | ||
| + | |||
| + | Evolutionary Morphing of Tryptophan Synthase: Functional Mechanisms for the Enzymatic Channeling of Indole.,Fleming JR, Schupfner M, Busch F, Basle A, Ehrmann A, Sterner R, Mayans O J Mol Biol. 2018 Oct 24. pii: S0022-2836(18)30606-5. doi:, 10.1016/j.jmb.2018.10.013. PMID:30367843<ref>PMID:30367843</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5n2p" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 35091]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Tryptophan synthase]] | [[Category: Tryptophan synthase]] | ||
[[Category: Fleming, J]] | [[Category: Fleming, J]] | ||
[[Category: Mayans, O]] | [[Category: Mayans, O]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 07:18, 26 June 2019
Sulfolobus solfataricus Tryptophan Synthase A
| |||||||||||
