4j9j: Difference between revisions
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==Structure of designed HisF== | ==Structure of designed HisF== | ||
<StructureSection load='4j9j' size='340' side='right' caption='[[4j9j]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4j9j' size='340' side='right'caption='[[4j9j]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4j9j]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4j9j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J9J FirstGlance]. <br> | ||
</td></tr> | </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=4j9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9j OCA], [https://pdbe.org/4j9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j9j RCSB], [https://www.ebi.ac.uk/pdbsum/4j9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9j ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HIS6_THEMA HIS6_THEMA] IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4j9j" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4j9j" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Indole-3-glycerol phosphate synthase|Indole-3-glycerol phosphate synthase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima MSB8]] | ||
[[Category: | [[Category: Rajendran C]] | ||
[[Category: | [[Category: Sperl J]] | ||
[[Category: | [[Category: Sterner R]] | ||
Revision as of 14:00, 24 November 2022
Structure of designed HisFStructure of designed HisF
Structural highlights
FunctionHIS6_THEMA IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013] Publication Abstract from PubMedIt has been postulated that the ubiquitous (betaalpha)8-barrel enzyme fold has evolved by duplication and fusion of an ancestral (betaalpha)4-half-barrel. We have previously reconstructed this process in the laboratory by fusing two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF). The resulting construct HisF-CC was stepwise stabilized to Sym1 and Sym2, which are extremely robust but catalytically inert proteins. Here, we report on the generation of a circular permutant of Sym2 and the establishment of a sugar isomerization reaction on its scaffold. Our results demonstrate that duplication and mutagenesis of (betaalpha)4-half-barrels can readily lead to a stable and catalytically active (betaalpha)8-barrel enzyme. Establishing catalytic activity on an artificial (betaalpha)-barrel protein designed from identical half-barrels.,Sperl JM, Rohweder B, Rajendran C, Sterner R FEBS Lett. 2013 Jun 24. pii: S0014-5793(13)00469-9. doi:, 10.1016/j.febslet.2013.06.022. PMID:23806364[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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